View source for 7w8m


==Crystal structure of Co-type nitrile hydratase mutant from Pseudomonas thermophila - A129R==
<StructureSection load='7w8m' size='340' side='right'caption='[[7w8m]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7w8m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudonocardia_thermophila Pseudonocardia thermophila] and [https://en.wikipedia.org/wiki/Pseudonocardia_thermophila_DSM_43832 Pseudonocardia thermophila DSM 43832]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W8M 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]] 2.6&#8491;</td></tr>
<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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7w8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w8m OCA], [https://pdbe.org/7w8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w8m RCSB], [https://www.ebi.ac.uk/pdbsum/7w8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w8m 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 ==
The narrow substrate scope limits the wide industrial application of enzymes. Here, we successfully broadened the substrate scope of a nitrile hydratase (NHase) through mutation of two tunnel entrance residues based on rational tunnel calculation. Two variants, with increased specific activity, especially toward bulky substrates, were obtained. Crystal structure analysis revealed that the mutations led to the expansion of the tunnel entrance, which might be conducive to substrate entry. More importantly, molecular dynamics simulations illustrated that the mutations introduced anti-correlated movements to the regions around the substrate tunnel and the active site, which would promote substrate access during the dynamic process of catalysis. Additionally, mutations on the corresponding tunnel entrance residues on other NHases also enhanced their activity toward bulky substrates. These results not only revealed that residues located at the enzyme surface were a key factor in enzyme catalytic performance, but also provided dynamic evidence for insight into enzyme substrate scope broadening.

Insight into the broadened substrate scope of nitrile hydratase by static and dynamic structure analysis.,Ma D, Cheng Z, Peplowski L, Han L, Xia Y, Hou X, Guo J, Yin D, Rao Y, Zhou Z Chem Sci. 2022 Jul 6;13(28):8417-8428. doi: 10.1039/d2sc02319a. eCollection 2022 , Jul 20. PMID:35919716<ref>PMID:35919716</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7w8m" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudonocardia thermophila]]
[[Category: Pseudonocardia thermophila DSM 43832]]
[[Category: Cheng ZY]]
[[Category: Fu K]]
[[Category: Hou XD]]
[[Category: Lai QP]]
[[Category: Ma D]]
[[Category: Peplowski L]]
[[Category: Rao YJ]]
[[Category: Yin DJ]]
[[Category: Zhou ZM]]