Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment (Q27639369)

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11 November 2019

title

Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment (English)

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11 November 2019

2

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Jennifer L. Martin

series ordinal

5

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1

Melissa A Edeling

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11 November 2019

author name string

Renata A Fabianek

series ordinal

3

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11 November 2019

Linda Thöny-Meyer

series ordinal

4

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11 November 2019

publication date

1 July 2002

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11 November 2019

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11 November 2019

volume

10

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11 November 2019

issue

7

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11 November 2019

page(s)

973-979

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Electron avenue: pathways of disulfide bond formation and isomerization

11 November 2019

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Oxidative protein folding is driven by the electron transport system

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In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG

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Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli

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Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade

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The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo

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7 January 2021

Characterization of the Bradyrhizobium japonicum CycY protein, a membrane-anchored periplasmic thioredoxin that may play a role as a reductant in the biogenesis of c-type cytochromes

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Characterization of the Escherichia coli CcmH protein reveals new insights into the redox pathway required for cytochrome c maturation

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Thioredoxin--a fold for all reasons

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Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B

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Crystal structure of the DsbA protein required for disulphide bond formation in vivo

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Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli

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A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units

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Lipocalins as a scaffold

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Bradyrhizobium japonicum TlpA, a novel membrane-anchored thioredoxin-like protein involved in the biogenesis of cytochrome aa3 and development of symbiosis

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Protein disulphide oxidoreductases in bacteria

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Structure of the soluble domain of a membrane-anchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties

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Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE).

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Processing of X-ray diffraction data collected in oscillation mode

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Improved methods for building protein models in electron density maps and the location of errors in these models

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7 January 2021

Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB

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7 January 2021

A reassessment of the range ofc-type cytochromes synthesized byEscherichia coli K-12

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7 January 2021

Prototype of a heme chaperone essential for cytochrome c maturation

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7 January 2021

Physical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation

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7 January 2021

Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution

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Identifiers

DOI

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11 November 2019

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