6ehc: Difference between revisions
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The | ==OmpUdeltaN (N-terminus deletion mutant of OmpU), outer membrane protein of Vibrio cholerae== | ||
<StructureSection load='6ehc' size='340' side='right'caption='[[6ehc]], [[Resolution|resolution]] 2.02Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ehc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EHC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6EHC FirstGlance]. <br> | |||
</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></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ehc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ehc OCA], [http://pdbe.org/6ehc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ehc RCSB], [http://www.ebi.ac.uk/pdbsum/6ehc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ehc 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ehc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Porin 3D structures|Porin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[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]] | |||
Latest revision as of 12:10, 11 November 2020
OmpUdeltaN (N-terminus deletion mutant of OmpU), outer membrane protein of Vibrio choleraeOmpUdeltaN (N-terminus deletion mutant of OmpU), outer membrane protein of Vibrio cholerae
Structural highlights
Function[OMPU_VIBC3] Forms pores that allow passive diffusion of small molecules across the outer membrane. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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