Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.
Identifieur interne : 000A49 ( Main/Exploration ); précédent : 000A48; suivant : 000A50Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.
Auteurs : W. Blodig [Suisse] ; A T Smith ; W A Doyle ; K. PiontekSource :
- Journal of molecular biology [ 0022-2836 ] ; 2001.
Descripteurs français
- KwdFr :
- Alcools benzyliques (métabolisme), Catalyse (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Escherichia coli (génétique), Hydroxylation (MeSH), Hème (composition chimique), Hème (métabolisme), Isoenzymes (composition chimique), Isoenzymes (génétique), Isoenzymes (métabolisme), Liaison hydrogène (MeSH), Modèles moléculaires (MeSH), Mutation (génétique), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme), Substitution d'acide aminé (génétique), Tryptophane (génétique), Tryptophane (métabolisme).
- MESH :
- composition chimique : Hème, Isoenzymes, Peroxidases, Protéines recombinantes.
- enzymologie : Phanerochaete.
- génétique : Escherichia coli, Isoenzymes, Mutation, Peroxidases, Phanerochaete, Substitution d'acide aminé, Tryptophane.
- métabolisme : Alcools benzyliques, Hème, Isoenzymes, Peroxidases, Protéines recombinantes, Tryptophane.
- Catalyse, Conformation des protéines, Cristallographie aux rayons X, Hydroxylation, Liaison hydrogène, Modèles moléculaires, Oxydoréduction.
English descriptors
- KwdEn :
- Amino Acid Substitution (genetics), Benzyl Alcohols (metabolism), Catalysis (MeSH), Crystallography, X-Ray (MeSH), Escherichia coli (genetics), Heme (chemistry), Heme (metabolism), Hydrogen Bonding (MeSH), Hydroxylation (MeSH), Isoenzymes (chemistry), Isoenzymes (genetics), Isoenzymes (metabolism), Models, Molecular (MeSH), Mutation (genetics), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Protein Conformation (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Tryptophan (genetics), Tryptophan (metabolism).
- MESH :
- chemical , chemistry : Heme, Isoenzymes, Peroxidases, Recombinant Proteins.
- chemical , genetics : Isoenzymes, Peroxidases, Tryptophan.
- chemical , metabolism : Benzyl Alcohols, Heme, Isoenzymes, Peroxidases, Recombinant Proteins, Tryptophan.
- enzymology : Phanerochaete.
- genetics : Amino Acid Substitution, Escherichia coli, Mutation, Phanerochaete.
- Catalysis, Crystallography, X-Ray, Hydrogen Bonding, Hydroxylation, Models, Molecular, Oxidation-Reduction, Protein Conformation.
Abstract
The heme enzyme lignin peroxidase (LiP) from the white rot fungus Phanerochaete chrysosporium contains a solvent exposed redox active tryptophan residue (Trp171) that carries a unique hydroxy group stereo-specifically attached to its C(beta) atom. A Trp171Phe mutant has no activity at all towards the substrate veratryl alcohol. The mechanism of veratryl alcohol oxidation involving beta-hydroxy-Trp171 is largely unknown. Here, we present the first crystal structures of LiP isozyme H8 at high resolution in its pristine non-hydroxylated form, of the C(beta)-hydroxylated form, and of the Trp171Phe mutant using recombinantly expressed and refolded protein produced from Escherichia coli. As a consequence, all structures are unglycosylated. Structural changes in response to the mutation are marginal and allow us to attribute the complete lack of activity exclusively to the absence of the redox active indole side-chain. The origin of the stereospecificity of the Trp171 hydroxylation can be explained on structural grounds. A reaction mechanism involving Trp171 is proposed and the possible function of the modification is discussed. Another important result regarding the ongoing debate on the co-ordination state of the heme iron in the resting state is that the iron is six co-ordinate in all cases the data being collected at room temperature. The mean distance from the iron to the distal water ligand is 2.18(+/-0.08) A. The radical scavenger orcinol was found to decrease radiation damage to the crystals, during data collection at room temperature.
DOI: 10.1006/jmbi.2000.4346
PubMed: 11162097
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Blodig</name><affiliation wicri:level="1"><nlm:affiliation>Institut für Biochemie, Eidgenössische Technische Hochschule (ETH), Universitätstrasse 16, Zürich, CH-8092, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Institut für Biochemie, Eidgenössische Technische Hochschule (ETH), Universitätstrasse 16, Zürich, CH-8092</wicri:regionArea><wicri:noRegion>CH-8092</wicri:noRegion></affiliation></author><author><name sortKey="Smith, A T" sort="Smith, A T" uniqKey="Smith A" first="A T" last="Smith">A T Smith</name></author><author><name sortKey="Doyle, W A" sort="Doyle, W A" uniqKey="Doyle W" first="W A" last="Doyle">W A Doyle</name></author><author><name sortKey="Piontek, K" sort="Piontek, K" uniqKey="Piontek K" first="K" last="Piontek">K. 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Blodig</name><affiliation wicri:level="1"><nlm:affiliation>Institut für Biochemie, Eidgenössische Technische Hochschule (ETH), Universitätstrasse 16, Zürich, CH-8092, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Institut für Biochemie, Eidgenössische Technische Hochschule (ETH), Universitätstrasse 16, Zürich, CH-8092</wicri:regionArea><wicri:noRegion>CH-8092</wicri:noRegion></affiliation></author><author><name sortKey="Smith, A T" sort="Smith, A T" uniqKey="Smith A" first="A T" last="Smith">A T Smith</name></author><author><name sortKey="Doyle, W A" sort="Doyle, W A" uniqKey="Doyle W" first="W A" last="Doyle">W A Doyle</name></author><author><name sortKey="Piontek, K" sort="Piontek, K" uniqKey="Piontek K" first="K" last="Piontek">K. 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A Trp171Phe mutant has no activity at all towards the substrate veratryl alcohol. The mechanism of veratryl alcohol oxidation involving beta-hydroxy-Trp171 is largely unknown. Here, we present the first crystal structures of LiP isozyme H8 at high resolution in its pristine non-hydroxylated form, of the C(beta)-hydroxylated form, and of the Trp171Phe mutant using recombinantly expressed and refolded protein produced from Escherichia coli. As a consequence, all structures are unglycosylated. Structural changes in response to the mutation are marginal and allow us to attribute the complete lack of activity exclusively to the absence of the redox active indole side-chain. The origin of the stereospecificity of the Trp171 hydroxylation can be explained on structural grounds. A reaction mechanism involving Trp171 is proposed and the possible function of the modification is discussed. Another important result regarding the ongoing debate on the co-ordination state of the heme iron in the resting state is that the iron is six co-ordinate in all cases the data being collected at room temperature. The mean distance from the iron to the distal water ligand is 2.18(+/-0.08) A. The radical scavenger orcinol was found to decrease radiation damage to the crystals, during data collection at room temperature.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11162097</PMID><DateCompleted><Year>2001</Year><Month>03</Month><Day>15</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>305</Volume><Issue>4</Issue><PubDate><Year>2001</Year><Month>Jan</Month><Day>26</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.</ArticleTitle><Pagination><MedlinePgn>851-61</MedlinePgn></Pagination><Abstract><AbstractText>The heme enzyme lignin peroxidase (LiP) from the white rot fungus Phanerochaete chrysosporium contains a solvent exposed redox active tryptophan residue (Trp171) that carries a unique hydroxy group stereo-specifically attached to its C(beta) atom. A Trp171Phe mutant has no activity at all towards the substrate veratryl alcohol. The mechanism of veratryl alcohol oxidation involving beta-hydroxy-Trp171 is largely unknown. Here, we present the first crystal structures of LiP isozyme H8 at high resolution in its pristine non-hydroxylated form, of the C(beta)-hydroxylated form, and of the Trp171Phe mutant using recombinantly expressed and refolded protein produced from Escherichia coli. As a consequence, all structures are unglycosylated. Structural changes in response to the mutation are marginal and allow us to attribute the complete lack of activity exclusively to the absence of the redox active indole side-chain. The origin of the stereospecificity of the Trp171 hydroxylation can be explained on structural grounds. A reaction mechanism involving Trp171 is proposed and the possible function of the modification is discussed. Another important result regarding the ongoing debate on the co-ordination state of the heme iron in the resting state is that the iron is six co-ordinate in all cases the data being collected at room temperature. The mean distance from the iron to the distal water ligand is 2.18(+/-0.08) A. The radical scavenger orcinol was found to decrease radiation damage to the crystals, during data collection at room temperature.</AbstractText><CopyrightInformation>Copyright 2001 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Blodig</LastName><ForeName>W</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Institut für Biochemie, Eidgenössische Technische Hochschule (ETH), Universitätstrasse 16, Zürich, CH-8092, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Smith</LastName><ForeName>A T</ForeName><Initials>AT</Initials></Author><Author ValidYN="Y"><LastName>Doyle</LastName><ForeName>W A</ForeName><Initials>WA</Initials></Author><Author ValidYN="Y"><LastName>Piontek</LastName><ForeName>K</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>1B80</AccessionNumber><AccessionNumber>1B82</AccessionNumber><AccessionNumber>1B85</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mol Biol</MedlineTA><NlmUniqueID>2985088R</NlmUniqueID><ISSNLinking>0022-2836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>MB4T4A711H</RegistryNumber><NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006900" MajorTopicYN="N">Hydroxylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>2</Month><Day>13</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>3</Month><Day>17</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>2</Month><Day>13</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11162097</ArticleId><ArticleId IdType="doi">10.1006/jmbi.2000.4346</ArticleId><ArticleId IdType="pii">S0022-2836(00)94346-8</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><noCountry><name sortKey="Doyle, W A" sort="Doyle, W A" uniqKey="Doyle W" first="W A" last="Doyle">W A Doyle</name><name sortKey="Piontek, K" sort="Piontek, K" uniqKey="Piontek K" first="K" last="Piontek">K. Piontek</name><name sortKey="Smith, A T" sort="Smith, A T" uniqKey="Smith A" first="A T" last="Smith">A T Smith</name></noCountry><country name="Suisse"><noRegion><name sortKey="Blodig, W" sort="Blodig, W" uniqKey="Blodig W" first="W" last="Blodig">W. Blodig</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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