Crystal structures of substrate binding site mutants of manganese peroxidase.
Identifieur interne : 000C17 ( Main/Exploration ); précédent : 000C16; suivant : 000C18Crystal structures of substrate binding site mutants of manganese peroxidase.
Auteurs : M. Sundaramoorthy [États-Unis] ; K. Kishi ; M H Gold ; T L PoulosSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1997.
Descripteurs français
- KwdFr :
- Acide édétique (métabolisme), Basidiomycota (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Manganèse (métabolisme), Modèles chimiques (MeSH), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Peroxidases (génétique), Peroxidases (métabolisme), Sites de fixation (génétique).
- MESH :
English descriptors
- KwdEn :
- Basidiomycota (MeSH), Binding Sites (genetics), Crystallography, X-Ray (MeSH), Edetic Acid (metabolism), Manganese (metabolism), Models, Chemical (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Peroxidases (genetics), Peroxidases (metabolism), Protein Conformation (MeSH).
- MESH :
- chemical , genetics : Peroxidases.
- chemical , metabolism : Edetic Acid, Manganese, Peroxidases.
- genetics : Binding Sites.
- Basidiomycota, Crystallography, X-Ray, Models, Chemical, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Conformation.
Abstract
Manganese peroxidase (MnP), an extracellular heme enzyme from the lignin-degrading basidiomycetous fungus, Phanerochaete chrysosporium, catalyzes the oxidation of MnII to MnIII. The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin model compounds. The proposed MnII binding site of MnP consists of a heme propionate, three acidic ligands (Glu-35, Glu-39, and Asp-179), and two water molecules. Using crystallographic methods, this binding site was probed by altering the amount of MnII bound to the protein. Crystals grown in the absence of MnII, or in the presence of EDTA, exhibited diminished electron density at this site. Crystals grown in excess MnII exhibited increased electron density at the proposed binding site but nowhere else in the protein. This suggests that there is only one major MnII binding site in MnP. Crystal structures of a single mutant (D179N) and a double mutant (E35Q,D179N) at this site were determined. The mutant structures lack a cation at the MnII binding site. The structure of the MnII binding site is altered significantly in both mutants, resulting in increased access to the solvent and substrate.
DOI: 10.1074/jbc.272.28.17574
PubMed: 9211904
Affiliations:
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Kishi</name></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author><author><name sortKey="Poulos, T L" sort="Poulos, T L" uniqKey="Poulos T" first="T L" last="Poulos">T L Poulos</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1997">1997</date><idno type="RBID">pubmed:9211904</idno><idno type="pmid">9211904</idno><idno type="doi">10.1074/jbc.272.28.17574</idno><idno type="wicri:Area/Main/Corpus">000C02</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C02</idno><idno type="wicri:Area/Main/Curation">000C02</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C02</idno><idno type="wicri:Area/Main/Exploration">000C02</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Crystal structures of substrate binding site mutants of manganese peroxidase.</title><author><name sortKey="Sundaramoorthy, M" sort="Sundaramoorthy, M" uniqKey="Sundaramoorthy M" first="M" last="Sundaramoorthy">M. Sundaramoorthy</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Biology & Biochemistry and Physiology & Biophysics, University of California, Irvine, California 92697-3900, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology & Biochemistry and Physiology & Biophysics, University of California, Irvine, California 92697-3900</wicri:regionArea><wicri:noRegion>California 92697-3900</wicri:noRegion></affiliation></author><author><name sortKey="Kishi, K" sort="Kishi, K" uniqKey="Kishi K" first="K" last="Kishi">K. Kishi</name></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author><author><name sortKey="Poulos, T L" sort="Poulos, T L" uniqKey="Poulos T" first="T L" last="Poulos">T L Poulos</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (MeSH)</term><term>Binding Sites (genetics)</term><term>Crystallography, X-Ray (MeSH)</term><term>Edetic Acid (metabolism)</term><term>Manganese (metabolism)</term><term>Models, Chemical (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Protein Conformation (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide édétique (métabolisme)</term><term>Basidiomycota (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Manganèse (métabolisme)</term><term>Modèles chimiques (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Sites de fixation (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Edetic Acid</term><term>Manganese</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Binding Sites</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peroxidases</term><term>Sites de fixation</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide édétique</term><term>Manganèse</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Basidiomycota</term><term>Crystallography, X-Ray</term><term>Models, Chemical</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Basidiomycota</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Modèles chimiques</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Manganese peroxidase (MnP), an extracellular heme enzyme from the lignin-degrading basidiomycetous fungus, Phanerochaete chrysosporium, catalyzes the oxidation of MnII to MnIII. The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin model compounds. The proposed MnII binding site of MnP consists of a heme propionate, three acidic ligands (Glu-35, Glu-39, and Asp-179), and two water molecules. Using crystallographic methods, this binding site was probed by altering the amount of MnII bound to the protein. Crystals grown in the absence of MnII, or in the presence of EDTA, exhibited diminished electron density at this site. Crystals grown in excess MnII exhibited increased electron density at the proposed binding site but nowhere else in the protein. This suggests that there is only one major MnII binding site in MnP. Crystal structures of a single mutant (D179N) and a double mutant (E35Q,D179N) at this site were determined. The mutant structures lack a cation at the MnII binding site. The structure of the MnII binding site is altered significantly in both mutants, resulting in increased access to the solvent and substrate.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9211904</PMID><DateCompleted><Year>1997</Year><Month>08</Month><Day>14</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>272</Volume><Issue>28</Issue><PubDate><Year>1997</Year><Month>Jul</Month><Day>11</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Crystal structures of substrate binding site mutants of manganese peroxidase.</ArticleTitle><Pagination><MedlinePgn>17574-80</MedlinePgn></Pagination><Abstract><AbstractText>Manganese peroxidase (MnP), an extracellular heme enzyme from the lignin-degrading basidiomycetous fungus, Phanerochaete chrysosporium, catalyzes the oxidation of MnII to MnIII. The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin model compounds. The proposed MnII binding site of MnP consists of a heme propionate, three acidic ligands (Glu-35, Glu-39, and Asp-179), and two water molecules. Using crystallographic methods, this binding site was probed by altering the amount of MnII bound to the protein. Crystals grown in the absence of MnII, or in the presence of EDTA, exhibited diminished electron density at this site. Crystals grown in excess MnII exhibited increased electron density at the proposed binding site but nowhere else in the protein. This suggests that there is only one major MnII binding site in MnP. Crystal structures of a single mutant (D179N) and a double mutant (E35Q,D179N) at this site were determined. The mutant structures lack a cation at the MnII binding site. The structure of the MnII binding site is altered significantly in both mutants, resulting in increased access to the solvent and substrate.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sundaramoorthy</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Molecular Biology & Biochemistry and Physiology & Biophysics, University of California, Irvine, California 92697-3900, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kishi</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>M H</ForeName><Initials>MH</Initials></Author><Author ValidYN="Y"><LastName>Poulos</LastName><ForeName>T L</ForeName><Initials>TL</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>1MNP</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber><NameOfSubstance UI="D008345">Manganese</NameOfSubstance></Chemical><Chemical><RegistryNumber>9G34HU7RV0</RegistryNumber><NameOfSubstance UI="D004492">Edetic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>J Biol Chem 1997 Oct 10;272(41):26072</RefSource></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004492" MajorTopicYN="N">Edetic Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>7</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>7</Month><Day>11</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>7</Month><Day>11</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9211904</ArticleId><ArticleId IdType="doi">10.1074/jbc.272.28.17574</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name><name sortKey="Kishi, K" sort="Kishi, K" uniqKey="Kishi K" first="K" last="Kishi">K. Kishi</name><name sortKey="Poulos, T L" sort="Poulos, T L" uniqKey="Poulos T" first="T L" last="Poulos">T L Poulos</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Sundaramoorthy, M" sort="Sundaramoorthy, M" uniqKey="Sundaramoorthy M" first="M" last="Sundaramoorthy">M. Sundaramoorthy</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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