Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment
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The chemistry and biochemistry of heme c: functional bases for covalent attachmentCytochrome c biogenesis System I: an intricate process catalyzed by a maturase supercomplex?Structure and Functional Properties of Bacillus subtilis Endospore Biogenesis Factor StoAAn Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression AnalysisDiversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Probing heme delivery processes in cytochrome c biogenesis System I.The acidic nature of the CcmG redox-active center is important for cytochrome c maturation in Escherichia coli.Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturationCrystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231.Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions.A thioredoxin-like/β-propeller protein maintains the efficiency of light harvesting in ArabidopsisThioredoxin-like proteins in F and other plasmid systemsCytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control.Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.Cytochrome c biogenesis System I.Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation.Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation.The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochrome c maturation.Disulfide isomerase activity of the dynamic, trimeric Proteus mirabilis ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB.Impact of selected amino acids of HP0377 (Helicobacter pylori thiol oxidoreductase) on its functioning as a CcmG (cytochrome c maturation) protein and Dsb (disulfide bond) isomerase.
P2860
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P2860
Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
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
name
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@ast
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@en
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@nl
type
label
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@ast
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@en
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@nl
prefLabel
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@ast
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@en
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@nl
P2093
P1433
P1476
Structure of CcmG/DsbE at 1.14 ...... minately oxidizing environment
@en
P2093
Linda Thöny-Meyer
Melissa A Edeling
Renata A Fabianek
P304
P356
10.1016/S0969-2126(02)00794-3
P577
2002-07-01T00:00:00Z