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=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ire]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ire]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudonocardia_thermophila Pseudonocardia thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IRE FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | ||
<tr | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ire FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ire OCA], [https://pdbe.org/1ire PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ire RCSB], [https://www.ebi.ac.uk/pdbsum/1ire PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ire ProSAT]</span></td></tr> | ||
</table> | |||
<table> | == Function == | ||
[https://www.uniprot.org/uniprot/NHAA_PSETH NHAA_PSETH] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ir/1ire_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ir/1ire_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<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;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1ire" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Pseudonocardia thermophila]] | [[Category: Pseudonocardia thermophila]] | ||
[[Category: Fushinobu | [[Category: Fushinobu S]] | ||
[[Category: Ito | [[Category: Ito K]] | ||
[[Category: Miyanaga | [[Category: Miyanaga A]] | ||
[[Category: Wakagi | [[Category: Wakagi T]] | ||
Latest revision as of 03:06, 21 November 2024
Crystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophilaCrystal Structure of Co-type nitrile hydratase from Pseudonocardia thermophila
Structural highlights
FunctionNHAA_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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