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TitleStructural insights into the secretin translocation channel in the type II secretion system.
Journal, issue, pagesNat Struct Mol Biol, Vol. 24, Issue 2, Page 177-183, Year 2017
Publish dateJan 9, 2017
AuthorsZhaofeng Yan / Meng Yin / Dandan Xu / Yongqun Zhu / Xueming Li /
PubMed AbstractThe secretin GspD of the type II secretion system (T2SS) forms a channel across the outer membrane in Gram-negative bacteria to transport substrates from the periplasm to the extracellular milieu. ...The secretin GspD of the type II secretion system (T2SS) forms a channel across the outer membrane in Gram-negative bacteria to transport substrates from the periplasm to the extracellular milieu. The lack of an atomic-resolution structure of the GspD channel hinders the investigation of substrate translocation mechanism of T2SS. Here we report cryo-EM structures of two GspD channels (∼1 MDa), from Escherichia coli K12 and Vibrio cholerae, at ∼3 Å resolution. The structures reveal a pentadecameric channel architecture, wherein three rings of GspD N domains form the periplasmic channel. The secretin domain constitutes a novel double β-barrel channel, with at least 60 β-strands in each barrel, and is stabilized by S domains. The outer membrane channel is sealed by β-strand-enriched gates. On the basis of the partially open state captured, we proposed a detailed gate-opening mechanism. Our structures provide a structural basis for understanding the secretin superfamily and the mechanism of substrate translocation in T2SS.
External linksNat Struct Mol Biol / PubMed:28067918
MethodsEM (single particle)
Resolution3.04 - 4.22 Å
Structure data

EMDB-6675, PDB-5wq7:
CryoEM structure of type II secretion system secretin GspD in E.coli K12
Method: EM (single particle) / Resolution: 3.04 Å

EMDB-6676, PDB-5wq8:
CryoEM structure of type II secretion system secretin GspD in Vibrio cholerae
Method: EM (single particle) / Resolution: 3.26 Å

EMDB-6677, PDB-5wq9:
CryoEM structure of type II secretion system secretin GspD G453A mutant in Vibrio cholerae
Method: EM (single particle) / Resolution: 4.22 Å

EMDB-6678:
CryoEM structure of type II secretion system cap deletion secretin GspD in Vibrio cholerae
Method: EM (single particle) / Resolution: 4.18 Å

Source
  • escherichia coli k-12 (bacteria)
  • Vibrio cholerae O1 (bacteria)
  • vibrio cholerae o1 biovar el tor str. n16961 (bacteria)
KeywordsPROTEIN TRANSPORT / Secretin family / C15 symmetry / T2SS / Secretin / G453A mutant

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