8ieu

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'''Unreleased structure'''
 
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The entry 8ieu is ON HOLD until Paper Publication
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==Crystal structure of the DUF2891 family protein CJ0554 from Campylobacter jejuni in space group P41212==
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<StructureSection load='8ieu' size='340' side='right'caption='[[8ieu]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8ieu]] is a 2 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=8IEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IEU FirstGlance]. <br>
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</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=8ieu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ieu OCA], [https://pdbe.org/8ieu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ieu RCSB], [https://www.ebi.ac.uk/pdbsum/8ieu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ieu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A2U0QSR5_CAMJU A0A2U0QSR5_CAMJU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8ieu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Campylobacter jejuni]]
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[[Category: Large Structures]]
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[[Category: Cho HY]]
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[[Category: Kim SY]]
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[[Category: Yoon SI]]

Revision as of 05:45, 31 May 2023

Crystal structure of the DUF2891 family protein CJ0554 from Campylobacter jejuni in space group P41212

PDB ID 8ieu

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