8iev: Difference between revisions

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'''Unreleased structure'''


The entry 8iev is ON HOLD  until Paper Publication
==Crystal structure of the DUF2891 family protein CJ0554 from Campylobacter jejuni in space group C2==
<StructureSection load='8iev' size='340' side='right'caption='[[8iev]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8iev]] is a 6 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=8IEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IEV FirstGlance]. <br>
</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=8iev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iev OCA], [https://pdbe.org/8iev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iev RCSB], [https://www.ebi.ac.uk/pdbsum/8iev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iev ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2U0QSR5_CAMJU A0A2U0QSR5_CAMJU]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Campylobacter jejuni is a pathogenic bacterium that causes enteritis and Guillain-Barre syndrome in humans. To identify a protein target for the development of a new therapeutic against C. jejuni infection, each gene product of C. jejuni must be functionally characterized. The cj0554 gene of C. jejuni encodes a DUF2891 family protein with unknown functions. To provide functional insights into CJ0554, we determined and analyzed the crystal structure of the CJ0554 protein. CJ0554 adopts an (alpha/alpha)(6)-barrel structure, which consists of an inner alpha(6) ring and an outer alpha(6) ring. CJ0554 assembles into a dimer in a unique top-to-top orientation that is not observed in its structural homologs, N-acetylglucosamine 2-epimerase superfamily members. Dimer formation was verified by analyzing CJ0554 and its ortholog protein through gel-filtration chromatography. The top of the CJ0554 monomer barrel harbors a cavity, which is connected to that of the second subunit in the dimer structure, generating a larger intersubunit cavity. This elongated cavity accommodates extra nonproteinaceous electron density, presumably as a pseudosubstrate, and is lined with generally catalytically active histidine residues that are invariant in CJ0554 orthologs. Therefore, we propose that the cavity functions as the active site of CJ0554.


Authors:  
Unique dimeric structure of the DUF2891 family protein CJ0554 from Campylobacter jejuni.,Kim SY, Cho HY, Yoon SI Biochem Biophys Res Commun. 2023 May 7;655:11-17. doi: , 10.1016/j.bbrc.2023.03.010. Epub 2023 Mar 6. PMID:36913761<ref>PMID:36913761</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8iev" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Campylobacter jejuni]]
[[Category: Large Structures]]
[[Category: Cho HY]]
[[Category: Kim SY]]
[[Category: Yoon SI]]
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