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2i4s

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Revision as of 08:22, 18 October 2017

PDZ domain of EpsC from Vibrio cholerae, residues 204-305

Structural highlights

2i4s is a 2 chain structure with sequence from "bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	epsC ("Bacillo virgola del Koch" Trevisan 1884)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GSPC_VIBCH] Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). Required for secretion of cholera toxin through the outer membrane.

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 type 2 secretion system (T2SS) occurring in Gram-negative bacteria is composed of 12-15 different proteins which form large assemblies spanning two membranes and secreting several virulence factors in folded state across the outer membrane. The T2SS component EpsC of Vibrio cholerae plays an important role in this machinery. While anchored in the inner membrane, by far the largest part of EpsC is periplasmic, containing a so-called homology region (HR) domain and a PDZ domain. Here we report studies on the structure and function of both periplasmic domains of EpsC. The crystal structures of two variants of the PDZ domain of EpsC from V. cholerae were determined at better than 2 A resolution. Compared to the short variant, the longer variant contains an additional N-terminal helix, and reveals a significant difference in the position of helix alphaB with respect to the beta-sheet. Both our structures show that the PDZ domain of EpsC adopts a more open form than in previously reported structures of other PDZ domains. Most interestingly, in the crystals of the short EpsC-PDZ domain the peptide binding groove interacts with an alpha-helix from a neighboring subunit burying approximately 921 A2 solvent accessible surface. This makes it possible that the PDZ domain of this bacterial protein binds proteins in a manner which is altogether different from that seen in any other PDZ domain so far. We also determined that the HR domain of EpsC is primarily responsible for the interaction with the secretin EpsD, while the PDZ is not, or much less, so. This new finding, together with studies of others, leads to the suggestion that the PDZ domain of EpsC may interact with exoproteins to be secreted while the HR domain plays a key role in linking the inner-membrane sub-complex of the T2SS in V. cholerae to the outer membrane secretin.

Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae.,Korotkov KV, Krumm B, Bagdasarian M, Hol WG J Mol Biol. 2006 Oct 20;363(2):311-21. Epub 2006 Aug 18. PMID:16978643^[1]

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

References

↑ Korotkov KV, Krumm B, Bagdasarian M, Hol WG. Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae. J Mol Biol. 2006 Oct 20;363(2):311-21. Epub 2006 Aug 18. PMID:16978643 doi:10.1016/j.jmb.2006.08.037

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2i4s"

@@ Line 1: / Line 1: @@
 ==PDZ domain of EpsC from Vibrio cholerae, residues 204-305==
 <StructureSection load='2i4s' size='340' side='right' caption='[[2i4s]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">epsC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</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=2i4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i4s OCA], [http://pdbe.org/2i4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i4s RCSB], [http://www.ebi.ac.uk/pdbsum/2i4s PDBsum]</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=2i4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i4s OCA], [http://pdbe.org/2i4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i4s RCSB], [http://www.ebi.ac.uk/pdbsum/2i4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2i4s ProSAT]</span></td></tr>
 </table>
 == Function ==

2i4s

From Proteopedia

Revision as of 08:22, 18 October 2017

PDZ domain of EpsC from Vibrio cholerae, residues 204-305

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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