6ehf: Difference between revisions

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<StructureSection load='6ehf' size='340' side='right' caption='[[6ehf]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
<StructureSection load='6ehf' size='340' side='right' caption='[[6ehf]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ehf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EHF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EHF FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ehf]] is a 1 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=6EHF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EHF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ompT, VC0395_A1445 ([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=6ehf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ehf OCA], [http://pdbe.org/6ehf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ehf RCSB], [http://www.ebi.ac.uk/pdbsum/6ehf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ehf ProSAT]</span></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=6ehf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ehf OCA], [http://pdbe.org/6ehf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ehf RCSB], [http://www.ebi.ac.uk/pdbsum/6ehf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ehf ProSAT]</span></td></tr>
</table>
</table>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Vibc3]]
[[Category: Pathania, M]]
[[Category: Pathania, M]]
[[Category: Berg, B van den]]
[[Category: Berg, B van den]]

Latest revision as of 11:49, 3 October 2018

OmpT (in-vitro folded), an outer membrane protein Vibrio cholerae (trimer form)OmpT (in-vitro folded), an outer membrane protein Vibrio cholerae (trimer form)

Structural highlights

6ehf is a 1 chain structure with sequence from Vibc3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:ompT, VC0395_A1445 (VIBC3)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Pathania M, Acosta-Gutierrez S, Bhamidimarri SP, Basle A, Winterhalter M, Ceccarelli M, van den Berg B. Unusual Constriction Zones in the Major Porins OmpU and OmpT from Vibrio cholerae. Structure. 2018 Apr 3. pii: S0969-2126(18)30091-1. doi:, 10.1016/j.str.2018.03.010. PMID:29657131 doi:http://dx.doi.org/10.1016/j.str.2018.03.010

6ehf, resolution 2.72Å

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OCA