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| | <StructureSection load='1uv7' size='340' side='right'caption='[[1uv7]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='1uv7' size='340' side='right'caption='[[1uv7]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uv7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UV7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uv7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UV7 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1uv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uv7 OCA], [https://pdbe.org/1uv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uv7 RCSB], [https://www.ebi.ac.uk/pdbsum/1uv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uv7 ProSAT]</span></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=1uv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uv7 OCA], [https://pdbe.org/1uv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uv7 RCSB], [https://www.ebi.ac.uk/pdbsum/1uv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uv7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GSPM_VIBCH GSPM_VIBCH] Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in the complex assembly and recruits EpsL resulting in a stable complex in the inner membrane. Provides thus a link between the energy-providing EpsE protein in the cytoplasm and the rest of the T2SS machinery.<ref>PMID:10322014</ref> <ref>PMID:10633109</ref> <ref>PMID:19251862</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillo virgola del koch trevisan 1884]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abendroth, J]] | |
| - | [[Category: Hol, W G.J]] | |
| - | [[Category: General secretion pathway]] | |
| - | [[Category: Transport]] | |
| | [[Category: Vibrio cholerae]] | | [[Category: Vibrio cholerae]] |
| | + | [[Category: Abendroth J]] |
| | + | [[Category: Hol WGJ]] |
| Structural highlights
Function
GSPM_VIBCH Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in the complex assembly and recruits EpsL resulting in a stable complex in the inner membrane. Provides thus a link between the energy-providing EpsE protein in the cytoplasm and the rest of the T2SS machinery.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The terminal branch of the general secretion pathway (Gsp or type II secretion system) is used by several pathogenic bacteria for the secretion of their virulence factors across the outer membrane. In these secretion systems, a complex of 12-15 Gsp proteins spans from the pore in the outer membrane via several associated signal or energy-transducing proteins in the inner membrane to a regulating ATPase in the cytosol. The human pathogen Vibrio cholerae uses such a system, called the Eps system, for the export of the cholera toxin and other virulence factors from its periplasm into the lumen of the gastrointestinal tract of the host. Here, we report the atomic structure of the periplasmic domain of the EpsM protein from V.cholerae, which is a part of the interface between the regulating part and the rest of the Eps system. The crystal structure was determined by Se-Met MAD phasing and the model was refined to 1.7A resolution. The monomer consists of two alphabetabeta-subdomains forming a sandwich of two alpha-helices and a four-stranded antiparallel beta-sheet. In the dimer, a deep cleft with a polar rim and a hydrophobic bottom made by conserved residues is located between the monomers. This cleft contains an extra electron density suggesting that this region might serve as a binding site of an unknown ligand or part of a protein partner. Unexpectedly, the fold of the periplasmic domain of EpsM is an undescribed circular permutation of the ferredoxin fold.
The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold.,Abendroth J, Rice AE, McLuskey K, Bagdasarian M, Hol WG J Mol Biol. 2004 Apr 30;338(3):585-96. PMID:15081815[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sandkvist M, Hough LP, Bagdasarian MM, Bagdasarian M. Direct interaction of the EpsL and EpsM proteins of the general secretion apparatus in Vibrio cholerae. J Bacteriol. 1999 May;181(10):3129-35. PMID:10322014 doi:10.1128/JB.181.10.3129-3135.1999
- ↑ Sandkvist M, Keith JM, Bagdasarian M, Howard SP. Two regions of EpsL involved in species-specific protein-protein interactions with EpsE and EpsM of the general secretion pathway in Vibrio cholerae. J Bacteriol. 2000 Feb;182(3):742-8. PMID:10633109 doi:10.1128/JB.182.3.742-748.2000
- ↑ Lybarger SR, Johnson TL, Gray MD, Sikora AE, Sandkvist M. Docking and assembly of the type II secretion complex of Vibrio cholerae. J Bacteriol. 2009 May;191(9):3149-61. PMID:19251862 doi:10.1128/JB.01701-08
- ↑ Abendroth J, Rice AE, McLuskey K, Bagdasarian M, Hol WG. The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold. J Mol Biol. 2004 Apr 30;338(3):585-96. PMID:15081815 doi:10.1016/j.jmb.2004.01.064
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