PDBsum entry 4ksr

Protein transport

PDB id: 4ksr

Contents

Protein chains

521 a.a.

PDB id:

4ksr

Name:

Protein transport

Title:

Crystal structure of the vibrio cholerae atpase gspe hexamer

Structure:

Type ii secretion system protein e, hemolysin-coregulated protein. Chain: a, b, c. Fragment: t2ss epse, p37093 residues 100-503, q02uz4. Synonym: t2ss protein e, cholera toxin secretion protein epse, general secretion pathway protein e, type ii traffic warden atpase. Engineered: yes. Other_details: chimeric protein

Source:

Vibrio cholerae o1, pseudomonas aeruginosa. Organism_taxid: 243277, 208963. Strain: atcc 39315 / el tor inaba n16961, ucbpp-pa14. Gene: epse, vc_2732, pa14_01030. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

4.20Å R-factor: 0.384 R-free: 0.376

Authors:

W.G.Hol,S.Turley,C.Y.Lu,Y.J.Park,S.T.Marionni,K.Lee,M.Patrick, M.Sandkvist,M.Bush,R.Shah

Key ref:

C.Lu et al. (2013). Hexamers of the type II secretion ATPase GspE from Vibrio cholerae with increased ATPase activity. Structure, 21, 1707-1717. PubMed id: 23954505 DOI: 10.1016/j.str.2013.06.027

Date:

17-May-13 Release date: 04-Sep-13

Protein chains

A0A0H2ZJ24  (A0A0H2ZJ24_PSEAB) -  Type VI secretion system tube protein Hcp from Pseudomonas aeruginosa (strain UCBPP-PA14)

Seq: 162 a.a.

Struc: 521 a.a.*

Protein chains

P37093  (GSPE_VIBCH) -  Type II secretion system ATPase E from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

Seq: 503 a.a.

Struc: 521 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.7.4.2.8 - protein-secreting ATPase.
• Reaction: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2013.06.027

Structure 21:1707-1717 (2013)

PubMed id: 23954505

Hexamers of the type II secretion ATPase GspE from Vibrio cholerae with increased ATPase activity.

C.Lu, S.Turley, S.T.Marionni, Y.J.Park, K.K.Lee, M.Patrick, R.Shah, M.Sandkvist, M.F.Bush, W.G.Hol.

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.