Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB.
about
Colicin biologyA universally applicable method of operon map prediction on minimally annotated genomes using conserved genomic context.The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicinsAllosteric β-propeller signalling in TolB and its manipulation by translocating colicinsInsight into the assembly mechanism in the supramolecular rings of the sodium-driven Vibrio flagellar motor from the structure of FlgTStructure ofNeisseria meningitidislipoprotein GNA1162Structural Evidence That Colicin A Protein Binds to a Novel Binding Site of TolA Protein in Escherichia coli PeriplasmTol-dependent macromolecule import through the Escherichia coli cell envelope requires the presence of an exposed TolA binding motif.The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factorPolar localization of Escherichia coli chemoreceptors requires an intact Tol-Pal complexThe trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coliColicin A binds to a novel binding site of TolA in the Escherichia coli periplasm.Role of Pseudomonas putida tol-oprL gene products in uptake of solutes through the cytoplasmic membrane.Antibacterial toxin colicin N and phage protein G3p compete with TolB for a binding site on TolA.NlpD links cell wall remodeling and outer membrane invagination during cytokinesis in Escherichia coli.The flagellar basal body-associated protein FlgT is essential for a novel ring structure in the sodium-driven Vibrio motor.Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation.A natively unfolded toxin domain uses its receptor as a folding template.
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P2860
Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Mutational analysis of the Tol ...... raction between TolA and TolB.
@en
Mutational analysis of the Tol ...... raction between TolA and TolB.
@nl
type
label
Mutational analysis of the Tol ...... raction between TolA and TolB.
@en
Mutational analysis of the Tol ...... raction between TolA and TolB.
@nl
prefLabel
Mutational analysis of the Tol ...... raction between TolA and TolB.
@en
Mutational analysis of the Tol ...... raction between TolA and TolB.
@nl
P2093
P2860
P1476
Mutational analysis of the Tol ...... raction between TolA and TolB.
@en
P2093
Anne Vianney
Jean Claude Lazzaroni
Jean François Dubuisson
P2860
P304
P356
10.1128/JB.184.16.4620-4625.2002
P407
P577
2002-08-01T00:00:00Z