4d65: Difference between revisions

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'''Unreleased structure'''


The entry 4d65 is ON HOLD  until Paper Publication
==Structure of porin Omp-Pst2 from P. stuartii; the asymmetric unit contains a dimer of trimers.==
<StructureSection load='4d65' size='340' side='right'caption='[[4d65]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4d65]] is a 6 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=4D65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D65 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FTT:3-HYDROXY-TETRADECANOIC+ACID'>FTT</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4d65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d65 OCA], [https://pdbe.org/4d65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d65 RCSB], [https://www.ebi.ac.uk/pdbsum/4d65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d65 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E3U905_PROST E3U905_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.


Authors: Nasrallah, C., Colletier, J.P.
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>


Description: Structure of porin Omp-Pst2 from Providencia stuartii
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4d65" style="background-color:#fffaf0;"></div>
 
==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 15:21, 20 December 2023

Structure of porin Omp-Pst2 from P. stuartii; the asymmetric unit contains a dimer of trimers.Structure of porin Omp-Pst2 from P. stuartii; the asymmetric unit contains a dimer of trimers.

Structural highlights

4d65 is a 6 chain structure with sequence from Providencia stuartii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

E3U905_PROST

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[1]

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

See Also

References

  1. 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. Porin self-association enables cell-to-cell contact in Providencia stuartii floating communities. 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 doi:http://dx.doi.org/10.1073/pnas.1714582115

4d65, resolution 2.20Å

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