View source for 4ob1


==Crystal Structure of Nitrile Hydratase from Pseudonocardia thermophila bound to Butaneboronic Acid via Co-crystallization==
<StructureSection load='4ob1' size='340' side='right'caption='[[4ob1]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ob1]] 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=4OB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OB1 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]] 1.631&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BUB:1-BUTANE+BORONIC+ACID'>BUB</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</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=4ob1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ob1 OCA], [https://pdbe.org/4ob1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ob1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ob1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ob1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NHAA_PSETH NHAA_PSETH] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nitrile hydratase (NHase) catalyzes the hydration of nitriles to their corresponding commercially valuable amides at ambient temperatures and physiological pH. Several reaction mechanisms have been proposed for NHase enzymes; however, the source of the nucleophile remains a mystery. Boronic acids have been shown to be potent inhibitors of numerous hydrolytic enzymes due to the open shell of boron, which allows it to expand from a trigonal planar (sp(2)) form to a tetrahedral form (sp(3)). Therefore, we examined the inhibition of the Co-type NHase from Pseudonocardia thermophila JCM 3095 (PtNHase) by boronic acids via kinetics and X-ray crystallography. Both 1-butaneboronic acid (BuBA) and phenylboronic acid (PBA) function as potent competitive inhibitors of PtNHase. X-ray crystal structures for BuBA and PBA complexed to PtNHase were solved and refined at 1.5, 1.6, and 1.2 A resolution. The resulting PtNHase-boronic acid complexes represent a "snapshot" of reaction intermediates and implicate the cysteine-sulfenic acid ligand as the catalytic nucleophile, a heretofore unknown role for the alphaCys(113)-OH sulfenic acid ligand. Based on these data, a new mechanism of action for the hydration of nitriles by NHase is presented.

The active site sulfenic acid ligand in nitrile hydratases can function as a nucleophile.,Martinez S, Wu R, Sanishvili R, Liu D, Holz R J Am Chem Soc. 2014 Jan 29;136(4):1186-9. doi: 10.1021/ja410462j. Epub 2014 Jan, 13. PMID:24383915<ref>PMID:24383915</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ob1" style="background-color:#fffaf0;"></div>

==See Also==
*[[Nitrile hydratase|Nitrile hydratase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudonocardia thermophila]]
[[Category: Dali L]]
[[Category: Richard H]]
[[Category: Rui W]]
[[Category: Ruslan S]]
[[Category: Salette M]]