Augmenting β-augmentation: structural basis of how BamB binds BamA and may support folding of outer membrane proteins
about
The structural biology of β-barrel membrane proteins: a summary of recent reportsCrystal Structure of BamD: An Essential Component of the β-Barrel Assembly Machinery of Gram-Negative BacteriaStructural Basis of Outer Membrane Protein Biogenesis in BacteriaCrystal Structure of -Barrel Assembly Machinery BamCD Protein ComplexCrystal Structure of BamB from Pseudomonas aeruginosa and Functional Evaluation of Its Conserved Structural FeaturesCrystallographic analysis of the C-terminal domain of theEscherichia colilipoprotein BamCStructural insight into the biogenesis of β-barrel membrane proteinsStructural basis for the interaction of BamB with the POTRA3-4 domains of BamAStructure of the BAM complex and its implications for biogenesis of outer-membrane proteinsThe β-barrel assembly machinery in motion.Structural snapshots of the β-barrel assembly machinery.The TamB ortholog of Borrelia burgdorferi interacts with the β-barrel assembly machine (BAM) complex protein BamAOuter membrane protein biogenesis in Gram-negative bacteriaComputational redesign of the lipid-facing surface of the outer membrane protein OmpA.Characterization of the β-barrel assembly machine accessory lipoproteins from Borrelia burgdorferi.The β-barrel membrane protein insertase machinery from Gram-negative bacteria.Inhibition of the β-barrel assembly machine by a peptide that binds BamD.Structure-function analysis reveals that the Pseudomonas aeruginosa Tps4 two-partner secretion system is involved in CupB5 translocation.Crystal structure of BamB bound to a periplasmic domain fragment of BamA, the central component of the β-barrel assembly machineA comprehensive analysis of the Omp85/TpsB protein superfamily structural diversity, taxonomic occurrence, and evolution.Lateral opening and exit pore formation are required for BamA functionIn vivo roles of BamA, BamB and BamD in the biogenesis of BamA, a core protein of the β-barrel assembly machine of Escherichia coli.Refolding, crystallization and preliminary X-ray crystallographic studies of the β-barrel domain of BamA, a membrane protein essential for outer membrane protein biogenesisbam Lipoproteins Assemble BamA in vitro.The major outer sheath protein (Msp) of Treponema denticola has a bipartite domain architecture and exists as periplasmic and outer membrane-spanning conformersDeciphering the roles of BamB and its interaction with BamA in outer membrane biogenesis, T3SS expression and virulence in SalmonellaThe bacterial outer membrane β-barrel assembly machinery.Genetic, biochemical, and molecular characterization of the polypeptide transport-associated domain of Escherichia coli BamA.BB0324 and BB0028 are constituents of the Borrelia burgdorferi β-barrel assembly machine (BAM) complex.Assembly of the β-Barrel Outer Membrane Proteins in Gram-Negative Bacteria, Mitochondria, and Chloroplasts.Substitutions in the BamA β-barrel domain overcome the conditional lethal phenotype of a ΔbamB ΔbamE strain of Escherichia coliThe Bam machine: a molecular cooper.The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of β-barrel assembly.The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coliSequential and spatially restricted interactions of assembly factors with an autotransporter beta domain.The virulence factor PEB4 (Cj0596) and the periplasmic protein Cj1289 are two structurally related SurA-like chaperones in the human pathogen Campylobacter jejuniFitting the Pieces of the β-Barrel Assembly Machinery ComplexThe Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine CoreThe structure of the β-barrel assembly machinery complex.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?
P2860
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P2860
Augmenting β-augmentation: structural basis of how BamB binds BamA and may support folding of outer membrane proteins
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
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
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@ast
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@en
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@nl
type
label
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@ast
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@en
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@nl
prefLabel
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@ast
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@en
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@nl
P1476
Augmenting β-augmentation: str ...... ing of outer membrane proteins
@en
P2093
Alexander Heuck
P304
P356
10.1016/J.JMB.2011.01.002
P407
P577
2011-03-11T00:00:00Z