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PDBsum entry 4k0u
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Protein transport
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PDB id
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4k0u
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References listed in PDB file
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Key reference
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Title
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Anatomy of secretin binding to the dickeya dadantii type ii secretion system pilotin.
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Authors
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S.Rehman,
S.Gu,
V.E.Shevchik,
R.W.Pickersgill.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2013,
69,
1381-1386.
[DOI no: ]
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PubMed id
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Abstract
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The secretins are a family of large multimeric channels in the outer membrane of
Gram-negative bacteria that are involved in protein export. In Dickeya dadantii
and many other pathogenic bacteria, the lipoprotein pilotin targets the secretin
subunits to the outer membrane, allowing a functional type II secretion system
to be assembled. Here, the crystal structure of the C-terminal peptide of the
secretin subunit bound to its cognate pilotin is reported. In solution, this
C-terminal region of the secretin is nonstructured. The secretin peptide folds
on binding to the pilotin to form just under four turns of α-helix which bind
tightly up against the first helix of the pilotin so that the hydrophobic
residues of the secretin helix can bind to the hydrophobic surface of the
pilotin. The secretin helix binds parallel to the first part of the fourth helix
of the pilotin. An N-capping aspartate encourages helix formation and binding by
interacting favourably with the helix dipole of the helical secretin peptide.
The structure of the secretin-pilotin complex of the phytopathogenic
D. dadantii described here is a paradigm for this interaction in the OutS-PulS
family of pilotins, which is essential for the correct assembly of the type II
secretion system of several potent human adversaries, including
enterohaemorrhagic Escherichia coli and Klebsiella oxytoca.
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Secondary reference #1
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Title
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Structural and functional insights into the pilotin-Secretin complex of the type ii secretion system.
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Authors
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S.Gu,
S.Rehman,
X.Wang,
V.E.Shevchik,
R.W.Pickersgill.
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Ref.
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Plos Pathog, 2012,
8,
e1002531.
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PubMed id
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