2zcf

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[[Image:2zcf.png|left|200px]]
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==Mutational study on Alpha-Gln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771==
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<StructureSection load='2zcf' size='340' side='right' caption='[[2zcf]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2zcf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZCF FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
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<tr><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>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ahj|1ahj]], [[2ahj|2ahj]], [[2cyz|2cyz]], [[2cz0|2cz0]], [[2cz1|2cz1]], [[2d0q|2d0q]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nthA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 Rhodococcus erythropolis]), nthB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 Rhodococcus erythropolis])</td></tr>
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<tr><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>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zcf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zcf RCSB], [http://www.ebi.ac.uk/pdbsum/2zcf PDBsum], [http://www.topsan.org/Proteins/RSGI/2zcf TOPSAN]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zc/2zcf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Nitrile hydratase (NHase) from Rhodococcus sp. N771 is a non-heme iron enzyme having post-translationally modified cysteine ligands, alphaCys112-SO2H and alphaCys114-SOH. We replaced alphaGln90, which is conserved in all known NHases and involved in the hydrogen-bond network around the catalytic center, with glutamic acid or asparagine. The kcat of alphaQ90E and alphaQ90N mutants decreased to 24% and 5% that of wild type respectively, but the effect of mutations on Km was not very significant. In both mutants, the alphaCys114-SOH modification appeared to be responsible for the catalysis as in native NHase. We crystallized the nitrosylated alphaQ90N mutant and determined its structure at a resolution of 1.43 A. The structure was basically identical to that of native nitrosylated NHase except for the mutated site and its vicinity. The structural difference between native and alphaQ90N mutant NHases suggested the importance of the hydrogen bond networks between alphaGln90 and the iron center for the catalytic activity.
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{{STRUCTURE_2zcf| PDB=2zcf | SCENE= }}
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Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771.,Takarada H, Kawano Y, Hashimoto K, Nakayama H, Ueda S, Yohda M, Kamiya N, Dohmae N, Maeda M, Odaka M Biosci Biotechnol Biochem. 2006 Apr;70(4):881-9. PMID:16636455<ref>PMID:16636455</ref>
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===Mutational study on Alpha-Gln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_16636455}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2zcf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCF OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:016636455</ref><references group="xtra"/>
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[[Category: Nitrile hydratase]]
[[Category: Nitrile hydratase]]
[[Category: Rhodococcus erythropolis]]
[[Category: Rhodococcus erythropolis]]

Revision as of 04:58, 2 October 2014

Mutational study on Alpha-Gln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771

2zcf, resolution 1.43Å

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