5n9h

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<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=5n9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n9h OCA], [http://pdbe.org/5n9h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n9h RCSB], [http://www.ebi.ac.uk/pdbsum/5n9h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n9h 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=5n9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n9h OCA], [http://pdbe.org/5n9h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n9h RCSB], [http://www.ebi.ac.uk/pdbsum/5n9h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n9h ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5n9h" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 06:09, 8 March 2018

STRUCTURE OF 283-LGNY-286, THE STERIC ZIPPER THAT SUPPORTS THE SELF-ASSOCIATION OF P. STUARTII OMP-PST2 INTO DIMERS OF TRIMERS

5n9h, resolution 1.00Å

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