6ehb: Difference between revisions

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-'''Unreleased structure'''
-The entry 6ehb is ON HOLD  until Paper Publication
+==OmpU, an outer membrane protein, of Vibrio cholerae==
+<StructureSection load='6ehb' size='340' side='right' caption='[[6ehb]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ehb]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibc3 Vibc3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EHB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EHB FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ompU, VC0395_A0162, VC395_0650 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=345073 VIBC3])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ehb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ehb OCA], [http://pdbe.org/6ehb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ehb RCSB], [http://www.ebi.ac.uk/pdbsum/6ehb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ehb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/OMPU_VIBC3 OMPU_VIBC3]] Forms pores that allow passive diffusion of small molecules across the outer membrane.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The outer membranes (OM) of many Gram-negative bacteria contain general porins, which form nonspecific, large-diameter channels for the diffusional uptake of small molecules required for cell growth and function. While the porins of Enterobacteriaceae (e.g., E. coli OmpF and OmpC) have been extensively characterized structurally and biochemically, much less is known about their counterparts in Vibrionaceae. Vibrio cholerae, the causative agent of cholera, has two major porins, OmpU and OmpT, for which no structural information is available despite their importance for the bacterium. Here we report high-resolution X-ray crystal structures of V. cholerae OmpU and OmpT complemented with molecular dynamics simulations. While similar overall to other general porins, the channels of OmpU and OmpT have unusual constrictions that create narrower barriers for small-molecule permeation and change the internal electric fields of the channels. Together with electrophysiological and in vitro transport data, our results illuminate small-molecule uptake within the Vibrionaceae.
-Authors:
+Unusual Constriction Zones in the Major Porins OmpU and OmpT from Vibrio cholerae.,Pathania M, Acosta-Gutierrez S, Bhamidimarri SP, Basle A, Winterhalter M, Ceccarelli M, van den Berg B Structure. 2018 Apr 3. pii: S0969-2126(18)30091-1. doi:, 10.1016/j.str.2018.03.010. PMID:29657131<ref>PMID:29657131</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 6ehb" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Porin|Porin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Vibc3]]
+[[Category: Pathania, M]]
+[[Category: Berg, B van den]]
+[[Category: Diffusion channel]]
+[[Category: Diffusion porin]]
+[[Category: Ion-channel]]
+[[Category: Ion-transport]]
+[[Category: Membrane beta barrel]]
+[[Category: Membrane protein]]
+[[Category: Non-specific porin]]
+[[Category: Ompf or ompc ortholog]]
+[[Category: Outer membrane protein]]
+[[Category: Porin]]