1ire: Difference between revisions
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==Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila== | ==Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila== | ||
<StructureSection load='1ire' size='340' side='right' caption='[[1ire]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1ire' size='340' side='right' caption='[[1ire]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrile_hydratase Nitrile hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.84 4.2.1.84] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrile_hydratase Nitrile hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.84 4.2.1.84] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ire FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ire OCA], [http://pdbe.org/1ire PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ire RCSB], [http://www.ebi.ac.uk/pdbsum/1ire PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ire FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ire OCA], [http://pdbe.org/1ire PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ire RCSB], [http://www.ebi.ac.uk/pdbsum/1ire PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ire ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ire ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 12:43, 4 October 2017
Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophilaCrystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila
Structural highlights
Function[NHAA_PSETH] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. [NHAB_PSETH] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of cobalt-containing nitrile hydratase from Pseudonocardia thermophila JCM 3095 at 1.8 A resolution revealed the structure of the noncorrin cobalt at the catalytic center. Two cysteine residues (alphaCys(111) and alphaCys(113)) coordinated to the cobalt were posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively, like in iron-containing nitrile hydratase. A tryptophan residue (betaTrp(72)), which may be involved in substrate binding, replaced the tyrosine residue of iron-containing nitrile hydratase. The difference seems to be responsible for the preference for aromatic nitriles rather than aliphatic ones of cobalt-containing nitrile hydratase. Crystal structure of cobalt-containing nitrile hydratase.,Miyanaga A, Fushinobu S, Ito K, Wakagi T Biochem Biophys Res Commun. 2001 Nov 16;288(5):1169-74. PMID:11700034[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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