View source for 5onu


==Trimeric OmpU structure==
<StructureSection load='5onu' size='340' side='right'caption='[[5onu]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5onu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ONU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ONU 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]] 2.22&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</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=5onu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5onu OCA], [https://pdbe.org/5onu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5onu RCSB], [https://www.ebi.ac.uk/pdbsum/5onu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5onu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OMPU_VIBCH OMPU_VIBCH] Forms pores that allow passive diffusion of small molecules across the outer membrane.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Vibrio cholerae causes a severe disease that kills thousands of people annually. The outer membrane protein OmpU is the most abundant outer membrane protein in V. cholerae, and has been identified as an important virulence factor that is involved in host-cell interaction and recognition, as well as being critical for the survival of the pathogenic V. cholerae in the host body and in harsh environments. The mechanism of these processes is not well understood owing to a lack of the structure of V. cholerae OmpU. Here, the crystal structure of the V. cholerae OmpU trimer is reported to a resolution of 2.2 A. The protomer forms a 16-beta-stranded barrel with a noncanonical N-terminal coil located in the lumen of the barrel that consists of residues Gly32-Ser42 and is observed to participate in forming the second gate in the pore. By mapping the published functional data onto the OmpU structure, the OmpU structure reinforces the notion that the long extracellular loop L4 with a beta-hairpin-like motif may be critical for host-cell binding and invasion, while L3, L4 and L8 are crucially implicated in phage recognition by V. cholerae.

Crystal structure of the outer membrane protein OmpU from Vibrio cholerae at 2.2 A resolution.,Li H, Zhang W, Dong C Acta Crystallogr D Struct Biol. 2018 Jan 1;74(Pt 1):21-29. doi:, 10.1107/S2059798317017697. Epub 2018 Jan 1. PMID:29372896<ref>PMID:29372896</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5onu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Porin 3D structures|Porin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Dong CJ]]
[[Category: Li HY]]