View source for 9wpo


==Crystal structure of the nitrilase superfamily protein CJ1056C from Campylobacter jejuni in space group P21==
<StructureSection load='9wpo' size='340' side='right'caption='[[9wpo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9wpo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9WPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9WPO 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]] 2.3&#8491;</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=9wpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9wpo OCA], [https://pdbe.org/9wpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9wpo RCSB], [https://www.ebi.ac.uk/pdbsum/9wpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9wpo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A5T0F3Q1_CAMJU A0A5T0F3Q1_CAMJU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nitrilase superfamily comprises enzymes that hydrolyze nonpeptide carbon-nitrogen bonds in nitriles and amides and contribute to diverse cellular processes, such as signaling, metabolism, and detoxification. These enzymes rely on the canonical Cys-Glu-Lys catalytic triad for their nitrilase or amidase activities. We identified a gene product of Campylobacter jejuni (CJ1056C) belonging to the nitrilase superfamily and determined its unique structure by X-ray crystallography in two crystal forms at resolutions of 2.3 A and 2.9 A. CJ1056C folds into a four-layered alphabetabetaalpha structure with a pocket, as observed in typical nitrilase superfamily proteins, such as Nit2 and aliphatic amidase. However, the catalytic triad of the nitrilase superfamily which is generally located at the base of the pocket, is disrupted in CJ1056C, with the catalytic residues cysteine and lysine replaced by glycine and glutamine, respectively, which are inherently unable to mediate hydrolysis. Furthermore, phylogenetic analysis revealed that CJ1056C and its orthologs from the Campylobacterota phylum form a unique cluster that is evolutionarily separate from catalytically active nitrilase superfamily proteins. Taken together, these findings establish CJ1056C as the first structurally characterized pseudoenzyme of the nitrilase superfamily, presumably lacking conventional nitrilase or amidase activities.

Structural analysis of the unique nitrilase superfamily protein CJ1056C from Campylobacter jejuni.,Ahn SY, Yoon SI Biochem Biophys Res Commun. 2025 Sep 20;785:152688. doi: , 10.1016/j.bbrc.2025.152688. PMID:41005285<ref>PMID:41005285</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9wpo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Campylobacter jejuni]]
[[Category: Large Structures]]
[[Category: Ahn SY]]
[[Category: Yoon SI]]