The Structure of Beef Liver Catalase
Identifieur interne : 004F24 ( Main/Exploration ); précédent : 004F23; suivant : 004F25The Structure of Beef Liver Catalase
Auteurs : Mathur R. N. Murthy [États-Unis] ; Thomas J. Reid Iii [États-Unis] ; Andrew Sicignano [États-Unis] ; Nobuo Tanaka [Japon] ; Michael G. Rossmann [États-Unis]Source :
- NATO Advanced Study Institutes Series [ 1389-2185 ]
Abstract
Abstract: The three-dimensional structure of beef liver catalase has been determined to 2.5 Å resolution by a combination of isomorphous and molecular replacement techniques. The tetrameric catalase molecule has 222 symmetry with one of its diads coincident with a crystallographic two fold axis. The known polypeptide sequence has been unambiguously fitted to the electron density map. The heme is well buried in a hydrophobic pocket, 20 Å below the surface of the molecule, and accessible through a hydrophobic channel. Residues that line the heme pocket belong to two different subunits. Tyr 357 is the proximal heme ligand and the catalytically important residues on the distal side are residues His 74 and Asn 147. The tertiary structure consists of four domains: an extended non-globular amino terminal arm which stabilizes the quaternary structure; an anti-parallel, eight- stranded β-barrel providing the residues on the distal side of the heme; a rather random “wrapping domain” around the subunit exterior including the proximal heme ligand; and a final α- helical structure.
Url:
DOI: 10.1007/978-94-009-7882-9_29
Affiliations:
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N." last="Murthy">Mathur R. N. Murthy</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, Purdue University, 47907, W. Lafayette, Indiana</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author><author><name sortKey="Reid Iii, Thomas J" sort="Reid Iii, Thomas J" uniqKey="Reid Iii T" first="Thomas J." last="Reid Iii">Thomas J. Reid Iii</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Uniformed Services, University of the Health Sciences, 20014, Bethesda, Maryland</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Sicignano, Andrew" sort="Sicignano, Andrew" uniqKey="Sicignano A" first="Andrew" last="Sicignano">Andrew Sicignano</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Charter International Oil Co., P.O. Box 5008, 77012, Houston, Texas</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author><author><name sortKey="Tanaka, Nobuo" sort="Tanaka, Nobuo" uniqKey="Tanaka N" first="Nobuo" last="Tanaka">Nobuo Tanaka</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Institute for Protein Research, Osaka University, Yamada-kami, Suita, 5311, Osaka</wicri:regionArea><wicri:noRegion>Osaka</wicri:noRegion></affiliation></author><author><name sortKey="Rossmann, Michael G" sort="Rossmann, Michael G" uniqKey="Rossmann M" first="Michael G." last="Rossmann">Michael G. Rossmann</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, Purdue University, 47907, W. Lafayette, Indiana</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="s" type="main" xml:lang="en">NATO Advanced Study Institutes Series</title><idno type="ISSN">1389-2185</idno><idno type="ISSN">1389-2185</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1389-2185</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The three-dimensional structure of beef liver catalase has been determined to 2.5 Å resolution by a combination of isomorphous and molecular replacement techniques. The tetrameric catalase molecule has 222 symmetry with one of its diads coincident with a crystallographic two fold axis. The known polypeptide sequence has been unambiguously fitted to the electron density map. The heme is well buried in a hydrophobic pocket, 20 Å below the surface of the molecule, and accessible through a hydrophobic channel. Residues that line the heme pocket belong to two different subunits. Tyr 357 is the proximal heme ligand and the catalytically important residues on the distal side are residues His 74 and Asn 147. The tertiary structure consists of four domains: an extended non-globular amino terminal arm which stabilizes the quaternary structure; an anti-parallel, eight- stranded β-barrel providing the residues on the distal side of the heme; a rather random “wrapping domain” around the subunit exterior including the proximal heme ligand; and a final α- helical structure.</div></front></TEI><affiliations><list><country><li>Japon</li><li>États-Unis</li></country><region><li>Indiana</li><li>Maryland</li><li>Texas</li></region></list><tree><country name="États-Unis"><region name="Indiana"><name sortKey="Murthy, Mathur R N" sort="Murthy, Mathur R N" uniqKey="Murthy M" first="Mathur R. N." last="Murthy">Mathur R. N. Murthy</name></region><name sortKey="Reid Iii, Thomas J" sort="Reid Iii, Thomas J" uniqKey="Reid Iii T" first="Thomas J." last="Reid Iii">Thomas J. Reid Iii</name><name sortKey="Rossmann, Michael G" sort="Rossmann, Michael G" uniqKey="Rossmann M" first="Michael G." last="Rossmann">Michael G. Rossmann</name><name sortKey="Sicignano, Andrew" sort="Sicignano, Andrew" uniqKey="Sicignano A" first="Andrew" last="Sicignano">Andrew Sicignano</name></country><country name="Japon"><noRegion><name sortKey="Tanaka, Nobuo" sort="Tanaka, Nobuo" uniqKey="Tanaka N" first="Nobuo" last="Tanaka">Nobuo Tanaka</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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