In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae.
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Exceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knivesStructure of the PilM-PilN Inner Membrane Type IV Pilus Biogenesis Complex from Thermus thermophilusStructure and assembly of an inner membrane platform for initiation of type IV pilus biogenesisCrystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspLMinor pseudopilin self-assembly primes type II secretion pseudopilus elongation.PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilAZinc coordination is essential for the function and activity of the type II secretion ATPase EpsEDistinct docking and stabilization steps of the Pseudopilus conformational transition path suggest rotational assembly of type IV pilus-like fibers.BfpL is essential for type IV bundle-forming pilus biogenesis and interacts with the periplasmic face of BfpCIdentification of surprisingly diverse type IV pili, across a broad range of gram-positive bacteria.The Type II secretion system delivers matrix proteins for biofilm formation by Vibrio cholerae.Function-related positioning of the type II secretion ATPase of Xanthomonas campestris pv. campestris.Oligomerization of EpsE coordinates residues from multiple subunits to facilitate ATPase activityDynamic interplay between the periplasmic and transmembrane domains of GspL and GspM in the type II secretion system.Secretins: dynamic channels for protein transport across membranesSecretion of TcpF by the Vibrio cholerae toxin-coregulated pilus biogenesis apparatus requires an N-terminal determinant.The type II secretion system: biogenesis, molecular architecture and mechanism.Structural insights into the Type II secretion nanomachine.The trans-envelope architecture and function of the type 2 secretion system: new insights raising new questions.Type IV Pilus Alignment Subcomplex Proteins PilN and PilO Form Homo- and Heterodimers in Vivo.The platform protein is essential for type IV pilus biogenesis.Cyclic Di-GMP and VpsR Induce the Expression of Type II Secretion in Vibrio cholerae.Pseudopilin residue E5 is essential for recruitment by the type 2 secretion system assembly platform.Novel Role for PilNO in Type IV Pilus Retraction Revealed by Alignment Subcomplex MutationsPhotobacterium damselae subsp. damselae major virulence factors Dly, plasmid-encoded HlyA, and chromosome-encoded HlyA are secreted via the type II secretion system
P2860
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P2860
In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae.
description
2011 nî lūn-bûn
@nan
2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@ast
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@en
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@nl
type
label
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@ast
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@en
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@nl
prefLabel
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@ast
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@en
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@nl
P2093
P2860
P1476
In vivo cross-linking of EpsG ...... ion system of Vibrio cholerae.
@en
P2093
Maria Sandkvist
Michael Bagdasarian
Miranda D Gray
Wim G J Hol
P2860
P304
P356
10.1111/J.1365-2958.2010.07487.X
P407
P577
2011-02-01T00:00:00Z