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4ksr

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Revision as of 11:10, 25 December 2014

Crystal Structure of the Vibrio cholerae ATPase GspE Hexamer

Structural highlights

4ksr is a 3 chain structure with sequence from Pseab. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4kss
Gene:	epsE, VC_2732, PA14_01030 (PSEAB)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

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

Publication Abstract from PubMed

The type II secretion system (T2SS), a multiprotein machinery spanning two membranes in Gram-negative bacteria, is responsible for the secretion of folded proteins from the periplasm across the outer membrane. The critical multidomain T2SS assembly ATPase GspEEpsE had not been structurally characterized as a hexamer. Here, four hexamers of Vibrio cholerae GspEEpsE are obtained when fused to Hcp1 as an assistant hexamer, as shown with native mass spectrometry. The enzymatic activity of the GspEEpsE-Hcp1 fusions is approximately 20 times higher than that of a GspEEpsE monomer, indicating that increasing the local concentration of GspEEpsE by the fusion strategy was successful. Crystal structures of GspEEpsE-Hcp1 fusions with different linker lengths reveal regular and elongated hexamers of GspEEpsE with major differences in domain orientation within subunits, and in subunit assembly. SAXS studies on GspEEpsE-Hcp1 fusions suggest that even further variability in GspEEpsE hexamer architecture is likely.

Hexamers of the Type II Secretion ATPase GspE from Vibrio cholerae with Increased ATPase Activity.,Lu C, Turley S, Marionni ST, Park YJ, Lee KK, Patrick M, Shah R, Sandkvist M, Bush MF, Hol WG Structure. 2013 Aug 13. pii: S0969-2126(13)00256-6. doi:, 10.1016/j.str.2013.06.027. PMID:23954505^[1]

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

References

↑ Lu C, Turley S, Marionni ST, Park YJ, Lee KK, Patrick M, Shah R, Sandkvist M, Bush MF, Hol WG. Hexamers of the Type II Secretion ATPase GspE from Vibrio cholerae with Increased ATPase Activity. Structure. 2013 Aug 13. pii: S0969-2126(13)00256-6. doi:, 10.1016/j.str.2013.06.027. PMID:23954505 doi:10.1016/j.str.2013.06.027

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ksr"

@@ Line 7: / Line 7: @@
 <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=4ksr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ksr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ksr RCSB], [http://www.ebi.ac.uk/pdbsum/4ksr PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/GSPE_VIBCH GSPE_VIBCH]] Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins. Required for secretion of cholera toxin through the outer membrane.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4ksr

From Proteopedia

Revision as of 11:10, 25 December 2014

Crystal Structure of the Vibrio cholerae ATPase GspE Hexamer

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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