4KSR

Crystal Structure of the Vibrio cholerae ATPase GspE Hexamer

Summary for 4KSR

• Entry DOI: 10.2210/pdb4ksr/pdb
• Related: 4KSS
• Descriptor: Type II secretion system protein E, Hemolysin-coregulated protein (1 entity in total)
• Functional Keywords: t2ss secretion atpase, epse, hexamer, c2 cyclic symmetry, protein transport
• Biological source: Vibrio cholerae O1; More
• Total number of polymer chains: 3
• Total formula weight: 192880.11

Authors

Hol, W.G.,Turley, S.,Lu, C.Y.,Park, Y.J.,Marionni, S.T.,Lee, K.,Patrick, M.,Sandkvist, M.,Bush, M.,Shah, R. (deposition date: 2013-05-17, release date: 2013-09-04, Last modification date: 2024-02-28)

Primary citation

Lu, C.,Turley, S.,Marionni, S.T.,Park, Y.J.,Lee, K.K.,Patrick, M.,Shah, R.,Sandkvist, M.,Bush, M.F.,Hol, W.G.
Hexamers of the Type II Secretion ATPase GspE from Vibrio cholerae with Increased ATPase Activity.
Structure, 21:1707-1717, 2013

PubMed Abstract: 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 GspE(EpsE) had not been structurally characterized as a hexamer. Here, four hexamers of Vibrio cholerae GspE(EpsE) are obtained when fused to Hcp1 as an assistant hexamer, as shown with native mass spectrometry. The enzymatic activity of the GspE(EpsE)-Hcp1 fusions is ∼20 times higher than that of a GspE(EpsE) monomer, indicating that increasing the local concentration of GspE(EpsE) by the fusion strategy was successful. Crystal structures of GspE(EpsE)-Hcp1 fusions with different linker lengths reveal regular and elongated hexamers of GspE(EpsE) with major differences in domain orientation within subunits, and in subunit assembly. SAXS studies on GspE(EpsE)-Hcp1 fusions suggest that even further variability in GspE(EpsE) hexamer architecture is likely.

PubMed: 23954505
DOI: 10.1016/j.str.2013.06.027

Experimental method

X-RAY DIFFRACTION (4.2 Å)