View source for 3wvd


==Crystal structure of Nitrile Hydratase mutant bR56K complexed with Trimethylacetonitrile, photo-activated for 50 min==
<StructureSection load='3wvd' size='340' side='right'caption='[[3wvd]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wvd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WVD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.18&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TAN:2,2-DIMETHYLPROPANENITRILE'>TAN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wvd OCA], [https://pdbe.org/3wvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wvd RCSB], [https://www.ebi.ac.uk/pdbsum/3wvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wvd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NHAA_RHOER NHAA_RHOER] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The reaction mechanism of nitrile hydratase (NHase) was investigated using time-resolved crystallography of the mutant NHase, in which betaArg56, strictly conserved and hydrogen bonded to the two post-translationally oxidized cysteine ligands, was replaced by lysine, and pivalonitrile was the substrate. The crystal structures of the reaction intermediates were determined at high resolution (1.2-1.3 A). In combination with FTIR analyses of NHase following hydration in H2 (18) O, we propose that the metal-coordinated substrate is nucleophilically attacked by the O(SO(-) ) atom of alphaCys114-SO(-) , followed by nucleophilic attack of the S(SO(-) ) atom by a betaArg56-activated water molecule to release the product amide and regenerate alphaCys114-SO(-) .

Time-Resolved Crystallography of the Reaction Intermediate of Nitrile Hydratase: Revealing a Role for the Cysteinesulfenic Acid Ligand as a Catalytic Nucleophile.,Yamanaka Y, Kato Y, Hashimoto K, Iida K, Nagasawa K, Nakayama H, Dohmae N, Noguchi K, Noguchi T, Yohda M, Odaka M Angew Chem Int Ed Engl. 2015 Sep 7;54(37):10763-7. doi: 10.1002/anie.201502731. PMID:26333053<ref>PMID:26333053</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wvd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Nitrile hydratase|Nitrile hydratase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodococcus erythropolis]]
[[Category: Hashimoto K]]
[[Category: Noguchi K]]
[[Category: Odaka M]]
[[Category: Yamanaka Y]]
[[Category: Yohda M]]