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3GR5

Periplasmic domain of the outer membrane secretin EscC from enteropathogenic E.coli (EPEC)

Summary for 3GR5
Entry DOI10.2210/pdb3gr5/pdb
Related3GR0 3GR1
DescriptorEscC, SULFATE ION (3 entities in total)
Functional Keywordssecretin, type iii secretion system, outer membrane, transport, membrane protein
Biological sourceEscherichia coli
Cellular locationCell outer membrane (By similarity): O52135
Total number of polymer chains1
Total formula weight18145.50
Authors
Yip, C.K.,Vockovic, M.,Strynadka, N.C.J. (deposition date: 2009-03-24, release date: 2009-05-19, Last modification date: 2024-11-27)
Primary citationSpreter, T.,Yip, C.K.,Sanowar, S.,Andre, I.,Kimbrough, T.G.,Vuckovic, M.,Pfuetzner, R.A.,Deng, W.,Yu, A.C.,Finlay, B.B.,Baker, D.,Miller, S.I.,Strynadka, N.C.
A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system.
Nat.Struct.Mol.Biol., 16:468-476, 2009
Cited by
PubMed Abstract: The type III secretion system (T3SS) is a macromolecular 'injectisome' that allows bacterial pathogens to transport virulence proteins into the eukaryotic host cell. This macromolecular complex is composed of connected ring-like structures that span both bacterial membranes. The crystal structures of the periplasmic domain of the outer membrane secretin EscC and the inner membrane protein PrgH reveal the conservation of a modular fold among the three proteins that form the outer membrane and inner membrane rings of the T3SS. This leads to the hypothesis that this conserved fold provides a common ring-building motif that allows for the assembly of the variably sized outer membrane and inner membrane rings characteristic of the T3SS. Using an integrated structural and experimental approach, we generated ring models for the periplasmic domain of EscC and placed them in the context of the assembled T3SS, providing evidence for direct interaction between the outer membrane and inner membrane ring components and an unprecedented span of the outer membrane secretin.
PubMed: 19396170
DOI: 10.1038/nsmb.1603
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

231029

건을2025-02-05부터공개중

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