Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 A resolution: a novel non-heme iron protein structure.
Identifieur interne : 004752 ( Main/Exploration ); précédent : 004751; suivant : 004753Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 A resolution: a novel non-heme iron protein structure.
Auteurs : RBID : pubmed:7666420English descriptors
- KwdEn :
- Amino Acid Sequence, Bacterial Proteins (chemistry), Computer Graphics, Crystallography, X-Ray, Cysteine (chemistry), Desulfovibrio (chemistry), Indium (chemistry), Iron (chemistry), Iron-Sulfur Proteins (chemistry), Models, Molecular, Molecular Sequence Data, Molecular Structure, Protein Structure, Secondary, Rubredoxins (chemistry), Sequence Alignment, Water (metabolism).
- MESH :
- chemical , chemistry : Bacterial Proteins, Cysteine, Indium, Iron, Iron-Sulfur Proteins, Rubredoxins.
- chemistry : Desulfovibrio.
- chemical , metabolism : Water.
- Amino Acid Sequence, Computer Graphics, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Molecular Structure, Protein Structure, Secondary, Sequence Alignment.
Abstract
The crystal structure of desulforedoxin from Desulfovibrio gigas, a new homo-dimeric (2 x 36 amino acids) non-heme iron protein, has been solved by the SIRAS method using the indium-substituted protein as the single derivative. The structure was refined to a crystallographic R-factor of 16.9% at 1.8 A resolution. Native desulforedoxin crystals were grown from either PEG 4K or lithium sulfate, with cell constants a = b = 42.18 A, c = 72.22 A (for crystals grown from PEG 4K), and they belong to space group P3(2)21. The indium-substituted protein crystallized isomorphously under the same conditions. The 2-fold symmetric dimer is firmly hydrogen bonded and folds as an incomplete beta-barrel with the two iron centers placed on opposite poles of the molecule. Each iron atom is coordinated to four cysteinyl residues in a distorted tetrahedral arrangement. Both iron atoms are 16 A apart but connected across the 2-fold axis by 14 covalent bonds along the polypeptide chain plus two hydrogen bonds. Desulforedoxin and rubredoxin share some structural features but show significant differences in terms of metal environment and water structure, which account for the known spectroscopic differences between rubredoxin and desulforedoxin.
PubMed: 7666420
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 A resolution: a novel non-heme iron protein structure.</title><author><name sortKey="Archer, M" uniqKey="Archer M">M Archer</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Tecnologia Química e Biológica, Oeiras, Portugal.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>Instituto de Tecnologia Química e Biológica, Oeiras</wicri:regionArea></affiliation></author><author><name sortKey="Huber, R" uniqKey="Huber R">R Huber</name></author><author><name sortKey="Tavares, P" uniqKey="Tavares P">P Tavares</name></author><author><name sortKey="Moura, I" uniqKey="Moura I">I Moura</name></author><author><name sortKey="Moura, J J" uniqKey="Moura J">J J Moura</name></author><author><name sortKey="Carrondo, M A" uniqKey="Carrondo M">M A Carrondo</name></author><author><name sortKey="Sieker, L C" uniqKey="Sieker L">L C Sieker</name></author><author><name sortKey="Legall, J" uniqKey="Legall J">J LeGall</name></author><author><name sortKey="Rom O, M J" uniqKey="Rom O M">M J Romão</name></author></titleStmt><publicationStmt><date when="1995">1995</date><idno type="RBID">pubmed:7666420</idno><idno type="pmid">7666420</idno><idno type="wicri:Area/Main/Corpus">004905</idno><idno type="wicri:Area/Main/Curation">004905</idno><idno type="wicri:Area/Main/Exploration">004752</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Bacterial Proteins (chemistry)</term><term>Computer Graphics</term><term>Crystallography, X-Ray</term><term>Cysteine (chemistry)</term><term>Desulfovibrio (chemistry)</term><term>Indium (chemistry)</term><term>Iron (chemistry)</term><term>Iron-Sulfur Proteins (chemistry)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Molecular Structure</term><term>Protein Structure, Secondary</term><term>Rubredoxins (chemistry)</term><term>Sequence Alignment</term><term>Water (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Cysteine</term><term>Indium</term><term>Iron</term><term>Iron-Sulfur Proteins</term><term>Rubredoxins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Desulfovibrio</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Water</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Computer Graphics</term><term>Crystallography, X-Ray</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Molecular Structure</term><term>Protein Structure, Secondary</term><term>Sequence Alignment</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The crystal structure of desulforedoxin from Desulfovibrio gigas, a new homo-dimeric (2 x 36 amino acids) non-heme iron protein, has been solved by the SIRAS method using the indium-substituted protein as the single derivative. The structure was refined to a crystallographic R-factor of 16.9% at 1.8 A resolution. Native desulforedoxin crystals were grown from either PEG 4K or lithium sulfate, with cell constants a = b = 42.18 A, c = 72.22 A (for crystals grown from PEG 4K), and they belong to space group P3(2)21. The indium-substituted protein crystallized isomorphously under the same conditions. The 2-fold symmetric dimer is firmly hydrogen bonded and folds as an incomplete beta-barrel with the two iron centers placed on opposite poles of the molecule. Each iron atom is coordinated to four cysteinyl residues in a distorted tetrahedral arrangement. Both iron atoms are 16 A apart but connected across the 2-fold axis by 14 covalent bonds along the polypeptide chain plus two hydrogen bonds. Desulforedoxin and rubredoxin share some structural features but show significant differences in terms of metal environment and water structure, which account for the known spectroscopic differences between rubredoxin and desulforedoxin.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">7666420</PMID><DateCreated><Year>1995</Year><Month>10</Month><Day>06</Day></DateCreated><DateCompleted><Year>1995</Year><Month>10</Month><Day>06</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>251</Volume><Issue>5</Issue><PubDate><Year>1995</Year><Month>Sep</Month><Day>1</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J. Mol. Biol.</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 A resolution: a novel non-heme iron protein structure.</ArticleTitle><Pagination><MedlinePgn>690-702</MedlinePgn></Pagination><Abstract><AbstractText>The crystal structure of desulforedoxin from Desulfovibrio gigas, a new homo-dimeric (2 x 36 amino acids) non-heme iron protein, has been solved by the SIRAS method using the indium-substituted protein as the single derivative. The structure was refined to a crystallographic R-factor of 16.9% at 1.8 A resolution. Native desulforedoxin crystals were grown from either PEG 4K or lithium sulfate, with cell constants a = b = 42.18 A, c = 72.22 A (for crystals grown from PEG 4K), and they belong to space group P3(2)21. The indium-substituted protein crystallized isomorphously under the same conditions. The 2-fold symmetric dimer is firmly hydrogen bonded and folds as an incomplete beta-barrel with the two iron centers placed on opposite poles of the molecule. Each iron atom is coordinated to four cysteinyl residues in a distorted tetrahedral arrangement. Both iron atoms are 16 A apart but connected across the 2-fold axis by 14 covalent bonds along the polypeptide chain plus two hydrogen bonds. Desulforedoxin and rubredoxin share some structural features but show significant differences in terms of metal environment and water structure, which account for the known spectroscopic differences between rubredoxin and desulforedoxin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Archer</LastName><ForeName>M</ForeName><Initials>M</Initials><Affiliation>Instituto de Tecnologia Química e Biológica, Oeiras, Portugal.</Affiliation></Author><Author ValidYN="Y"><LastName>Huber</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Tavares</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Moura</LastName><ForeName>I</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Moura</LastName><ForeName>J J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Carrondo</LastName><ForeName>M A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Sieker</LastName><ForeName>L C</ForeName><Initials>LC</Initials></Author><Author ValidYN="Y"><LastName>LeGall</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Romão</LastName><ForeName>M J</ForeName><Initials>MJ</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM 41482</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType>Journal Article</PublicationType><PublicationType>Research Support, Non-U.S. Gov't</PublicationType><PublicationType>Research Support, U.S. Gov't, P.H.S.</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>Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Rubredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>045A6V3VFX</RegistryNumber><NameOfSubstance>Indium</NameOfSubstance></Chemical><Chemical><RegistryNumber>059QF0KO0R</RegistryNumber><NameOfSubstance>Water</NameOfSubstance></Chemical><Chemical><RegistryNumber>72066-33-2</RegistryNumber><NameOfSubstance>desulforedoxin</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance>Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance>Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Bacterial 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MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Rubredoxins</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Water</DescriptorName><QualifierName MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>9</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7666420</ArticleId><ArticleId IdType="pii">S0022283685704652</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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