Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution
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Colicin biologyModel of the brain tumor-Pumilio translation repressor complexThe 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 FlgTCrystal structure of the enzyme CapF of Staphylococcus aureus reveals a unique architecture composed of two functional domainsOuter-membrane lipoprotein LpoB spans the periplasm to stimulate the peptidoglycan synthase PBP1BMolecular architecture of the 40S⋅eIF1⋅eIF3 translation initiation complexMolecular basis of bacterial outer membrane permeability revisitedA comprehensive analysis of the Omp85/TpsB protein superfamily structural diversity, taxonomic occurrence, and evolution.Strong decrease in invasive ability and outer membrane vesicle release in Crohn's disease-associated adherent-invasive Escherichia coli strain LF82 with the yfgL gene deleted.Structure of an apoptosome-procaspase-9 CARD complex.Tol-dependent macromolecule import through the Escherichia coli cell envelope requires the presence of an exposed TolA binding motif.Metagenomic analysis of Streptomyces lividans reveals host-dependent functional expression.Comparison of tertiary structures of proteins in protein-protein complexes with unbound forms suggests prevalence of allostery in signalling proteins.Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9.Colicin A binds to a novel binding site of TolA in the Escherichia coli periplasm.Colicin translocation across the Escherichia coli outer membrane.The physiology of bacterial cell division.Structural and functional aspects of the Helicobacter pylori secretome.Energy-dependent conformational change in the TolA protein of Escherichia coli involves its N-terminal domain, TolQ, and TolR.Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB.Antibacterial toxin colicin N and phage protein G3p compete with TolB for a binding site on TolA.Dual orientation of the outer membrane lipoprotein Pal in Escherichia coli.
P2860
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P2860
Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@ast
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@en
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@nl
type
label
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@ast
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@en
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@nl
prefLabel
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@ast
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@en
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@nl
P2093
P1433
P1476
Structure of the Escherichia c ...... D methods at 1.95 A resolution
@en
P2093
P304
P356
10.1016/S0969-2126(00)80062-3
P577
1999-10-15T00:00:00Z