Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
about
Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regenerationPreparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbBNMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbBStructure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid BilayerStructures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transferCatalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsDisulfide rearrangement triggered by translocon assembly controls lipopolysaccharide exportDiversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Disulfide bond formation involves a quinhydrone-type charge-transfer complex.Disulfide bond formation in prokaryotes: history, diversity and designFormation and transfer of disulphide bonds in living cells.Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria.Mechanism of the electron transfer catalyst DsbB from Escherichia coli.IcsA autotransporter passenger promotes increased fusion protein expression on the cell surface.Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD.Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility.Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways.Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy.A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidaseDisulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm.Disulfide bond formation system in Escherichia coli.Mechanisms of oxidative protein folding in the bacterial cell envelope.Direct observation of disulfide isomerization in a single protein.Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.Mutational alterations of the key cis proline residue that cause accumulation of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily.Role of the intramolecular disulfide bond in FlgI, the flagellar P-ring component of Escherichia coli.The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductasesReal-time monitoring of intermediates reveals the reaction pathway in the thiol-disulfide exchange between disulfide bond formation protein A (DsbA) and B (DsbB) on a membrane-immobilized quartz crystal microbalance (QCM) system.Reoxidation of the Thiol-Disulfide Oxidoreductase MdbA by a Bacterial Vitamin K Epoxide Reductase in the Biofilm-Forming Actinobacterium Actinomyces oris.DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre.Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis.Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli.Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in two subcellular compartments.Reactivities of quinone-free DsbB from Escherichia coli.
P2860
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P2860
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
@en
type
label
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
@en
prefLabel
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
@en
P2860
P356
P1433
P1476
Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
@en
P2093
Hiroshi Kadokura
Jon Beckwith
P2860
P304
P356
10.1093/EMBOJ/21.10.2354
P407
P577
2002-05-01T00:00:00Z