5nxr: Difference between revisions
New page: '''Unreleased structure''' The entry 5nxr is ON HOLD Authors: Colletier, J.P., Nasrallah, C. Description: Trimeric structure of Omp-Pst1, the major porin from Providencia stuartii [[Ca... |
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==Trimeric structure of Omp-Pst1, the major porin from Providencia stuartii== | |||
<StructureSection load='5nxr' size='340' side='right'caption='[[5nxr]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nxr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Providencia_stuartii Providencia stuartii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NXR 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]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5nxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nxr OCA], [https://pdbe.org/5nxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nxr RCSB], [https://www.ebi.ac.uk/pdbsum/5nxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nxr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E3U904_PROST E3U904_PROST] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The gram-negative pathogen Providencia stuartii forms floating communities within which adjacent cells are in apparent contact, before depositing as canonical surface-attached biofilms. Because porins are the most abundant proteins in the outer membrane of gram-negative bacteria, we hypothesized that they could be involved in cell-to-cell contact and undertook a structure-function relationship study on the two porins of P. stuartii, Omp-Pst1 and Omp-Pst2. Our crystal structures reveal that these porins can self-associate through their extracellular loops, forming dimers of trimers (DOTs) that could enable cell-to-cell contact within floating communities. Support for this hypothesis was obtained by studying the porin-dependent aggregation of liposomes and model cells. The observation that facing channels are open in the two porin structures suggests that DOTs could not only promote cell-to-cell contact but also contribute to intercellular communication. | |||
Porin self-association enables cell-to-cell contact in Providencia stuartii floating communities.,El-Khatib M, Nasrallah C, Lopes J, Tran QT, Tetreau G, Basbous H, Fenel D, Gallet B, Lethier M, Bolla JM, Pages JM, Vivaudou M, Weik M, Winterhalter M, Colletier JP Proc Natl Acad Sci U S A. 2018 Mar 6;115(10):E2220-E2228. doi:, 10.1073/pnas.1714582115. Epub 2018 Feb 23. PMID:29476011<ref>PMID:29476011</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5nxr" style="background-color:#fffaf0;"></div> | ||
[[Category: Colletier | |||
==See Also== | |||
*[[Porin 3D structures|Porin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Providencia stuartii]] | |||
[[Category: Colletier JP]] | |||
[[Category: Nasrallah C]] | |||
Latest revision as of 15:15, 22 November 2023
Trimeric structure of Omp-Pst1, the major porin from Providencia stuartiiTrimeric structure of Omp-Pst1, the major porin from Providencia stuartii
Structural highlights
FunctionPublication Abstract from PubMedThe gram-negative pathogen Providencia stuartii forms floating communities within which adjacent cells are in apparent contact, before depositing as canonical surface-attached biofilms. Because porins are the most abundant proteins in the outer membrane of gram-negative bacteria, we hypothesized that they could be involved in cell-to-cell contact and undertook a structure-function relationship study on the two porins of P. stuartii, Omp-Pst1 and Omp-Pst2. Our crystal structures reveal that these porins can self-associate through their extracellular loops, forming dimers of trimers (DOTs) that could enable cell-to-cell contact within floating communities. Support for this hypothesis was obtained by studying the porin-dependent aggregation of liposomes and model cells. The observation that facing channels are open in the two porin structures suggests that DOTs could not only promote cell-to-cell contact but also contribute to intercellular communication. Porin self-association enables cell-to-cell contact in Providencia stuartii floating communities.,El-Khatib M, Nasrallah C, Lopes J, Tran QT, Tetreau G, Basbous H, Fenel D, Gallet B, Lethier M, Bolla JM, Pages JM, Vivaudou M, Weik M, Winterhalter M, Colletier JP Proc Natl Acad Sci U S A. 2018 Mar 6;115(10):E2220-E2228. doi:, 10.1073/pnas.1714582115. Epub 2018 Feb 23. PMID:29476011[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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