The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan.
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In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactionsHybrid motor with H(+)- and Na(+)-driven components can rotate Vibrio polar flagella by using sodium ionsPolar flagellum biogenesis in Aeromonas hydrophilaColicin biologyBiogenesis and function of Porphyromonas gingivalis outer membrane vesiclesIntegrated Information and Prospects for Gliding Mechanism of the Pathogenic Bacterium Mycoplasma pneumoniae.Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliGInsights into the stator assembly of the Vibrio flagellar motor from the crystal structure of MotY.Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: Implications for peptidoglycan recognitionCrystallographic and Molecular Dynamics Analysis of Loop Motions Unmasking the Peptidoglycan-Binding Site in Stator Protein MotB of Flagellar MotorMechanism of anchoring of OmpA protein to the cell wall peptidoglycan of the gram-negative bacterial outer membraneMolecular Structure and Peptidoglycan Recognition of Mycobacterium tuberculosis ArfA (Rv0899)Evidence for two flagellar stators and their role in the motility of Pseudomonas aeruginosaThe complex flagellar torque generator of Pseudomonas aeruginosaMutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complexThe tetrameric MotA complex as the core of the flagellar motor stator from hyperthermophilic bacteriumMolecular basis of bacterial outer membrane permeability revisitedInsights into PG-Binding, Conformational Change, and Dimerization of the OmpA C-terminal Domains from Salmonella enterica serovar Typhimurium and Borrelia burgdorferi.Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA.TprC/D (Tp0117/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structureInsights into the structure and assembly of Escherichia coli outer membrane protein AAlternative folding pathways of the major porin OprF of Pseudomonas aeruginosa.Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of the periplasmic domain of outer membrane protein A from Acinetobacter baumannii.Mycobacterium tuberculosis Rv0899 defines a family of membrane proteins widespread in nitrogen-fixing bacteria.Factors affecting the folding of Pseudomonas aeruginosa OprF porin into the one-domain open conformerSurface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum.Pseudomonas aeruginosa porin OprF exists in two different conformationsTrimeric structure of major outer membrane proteins homologous to OmpA in Porphyromonas gingivalis.OmpA: a pore or not a pore? Simulation and modeling studies.Structure and function of bacterial outer membrane proteins: barrels in a nutshell.Aeromonas salmonicida possesses two genes encoding homologs of the major outer membrane protein, OmpAProtein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Organization of FliN subunits in the flagellar motor of Escherichia coliMutations alter the sodium versus proton use of a Bacillus clausii flagellar motor and confer dual ion use on Bacillus subtilis motors.Cryo-electron tomography elucidates the molecular architecture of Treponema pallidum, the syphilis spirocheteA Bacillus flagellar motor that can use both Na+ and K+ as a coupling ion is converted by a single mutation to use only Na+Unique constitution of photosystem I with a novel subunit in the cyanobacterium Gloeobacter violaceus PCC 7421.The regulated outer membrane protein Omp21 from Comamonas acidovorans is identified as a member of a new family of eight-stranded beta-sheet proteins by its sequence and properties.Molecular characterization of an outer membrane protein of Actinobacillus actinomycetemcomitans belonging to the OmpA family.Stoichiometry and turnover in single, functioning membrane protein complexes.
P2860
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P2860
The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh-hant
name
The C-terminal sequence conser ...... se domains with peptidoglycan.
@en
The C-terminal sequence conser ...... se domains with peptidoglycan.
@nl
type
label
The C-terminal sequence conser ...... se domains with peptidoglycan.
@en
The C-terminal sequence conser ...... se domains with peptidoglycan.
@nl
prefLabel
The C-terminal sequence conser ...... se domains with peptidoglycan.
@en
The C-terminal sequence conser ...... se domains with peptidoglycan.
@nl
P1476
The C-terminal sequence conser ...... se domains with peptidoglycan.
@en
P2093
Vanderleyden J
P304
P356
10.1111/J.1365-2958.1994.TB01021.X
P407
P577
1994-04-01T00:00:00Z