View source for 7qov


==The wild type nitrile hydratase from Geobacillus pallidus==
<StructureSection load='7qov' size='340' side='right'caption='[[7qov]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7qov]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeribacillus_pallidus Aeribacillus pallidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QOV 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]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3CO:COBALT+(III)+ION'>3CO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=7qov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qov OCA], [https://pdbe.org/7qov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qov RCSB], [https://www.ebi.ac.uk/pdbsum/7qov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qov ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q84FS5_9BACI Q84FS5_9BACI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nitrile hydratases (NHases) are important biocatalysts for the enzymatic conversion of nitriles to industrially-important amides such as acrylamide and nicotinamide. Although thermostability in this enzyme class is generally low, there is not sufficient understanding of its basis for rational enzyme design. The gene expressing the Co-type NHase from the moderate thermophile, Geobacillus pallidus RAPc8 (NRRL B-59396), was subjected to random mutagenesis. Four mutants were selected that were 3 to 15-fold more thermostable than the wild-type NHase, resulting in a 3.4-7.6 âkJ/mol increase in the activation energy of thermal inactivation at 63 â degrees C. High resolution X-ray crystal structures (1.15-1.80 âA) were obtained of the wild-type and four mutant enzymes. Mutant 9E, with a resolution of 1.15 âA, is the highest resolution crystal structure obtained for a nitrile hydratase to date. Structural comparisons between the wild-type and mutant enzymes illustrated the importance of salt bridges and hydrogen bonds in enhancing NHase thermostability. These additional interactions variously improved thermostability by increased intra- and inter-subunit interactions, preventing cooperative unfolding of alpha-helices and stabilising loop regions. Some hydrogen bonds were mediated via a water molecule, specifically highlighting the significance of structured water molecules in protein thermostability. Although knowledge of the mutant structures makes it possible to rationalize their behaviour, it would have been challenging to predict in advance that these mutants would be stabilising.

Engineering enhanced thermostability into the Geobacillus pallidus nitrile hydratase.,Van Wyk JC, Sewell BT, Danson MJ, Tsekoa TL, Sayed MF, Cowan DA Curr Res Struct Biol. 2022 Aug 19;4:256-270. doi: 10.1016/j.crstbi.2022.07.002. , eCollection 2022. PMID:36106339<ref>PMID:36106339</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7qov" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aeribacillus pallidus]]
[[Category: Large Structures]]
[[Category: Cowan DA]]
[[Category: Danson MJ]]
[[Category: Sayed MF]]
[[Category: Sewell BT]]
[[Category: Tsekoa TL]]
[[Category: Van Wyk JC]]