(Q27642487)

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Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis

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scholarly article

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Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis (English)

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Gram-negative bacteria

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gram-positive bacteria

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Mycobacterium tuberculosis

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protein structure

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David Eisenberg

7

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author name string

Celia W Goulding

1

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Marcin I Apostol

2

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Stefan Gleiter

3

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Angineh Parseghian

4

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James Bardwell

5

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Marila Gennaro

6

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language of work or name

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publication date

30 January 2004

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Journal of Biological Chemistry

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279

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3516-24

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5

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Thioredoxin--a fold for all reasons

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Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily

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Protein folding in the bacterial periplasm

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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

1 reference

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21 January 2018

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.

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https://api.crossref.org/works/10.1074%2FJBC.M311833200

21 January 2018

Identification of a protein required for disulfide bond formation in vivo.

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21 January 2018

In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.

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21 January 2018

Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo

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Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae

1 reference

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The tcp gene cluster of Vibrio cholerae.

1 reference

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Influence of the conserved disulphide bond, exposed to the putative binding pocket, on the structure and function of the immunoglobulin-like molecular chaperone Caf1M of Yersinia pestis

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DsbA: a protein-folding catalyst contributing to bacterial virulence

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DsbA is required for stability of the type IV pilin of enteropathogenic escherichia coli.

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Global epidemiology of tuberculosis. Morbidity and mortality of a worldwide epidemic

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Global surveillance for antituberculosis-drug resistance, 1994-1997. World Health Organization-International Union against Tuberculosis and Lung Disease Working Group on Anti-Tuberculosis Drug Resistance Surveillance.

1 reference

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The TB structural genomics consortium: providing a structural foundation for drug discovery.

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Structural genomics of Mycobacterium tuberculosis: a preliminary report of progress at UCLA

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Cloning, expression and significance of MPT53 for identification of secreted proteins of Mycobacterium tuberculosis

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Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin

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The CCP4 suite: programs for protein crystallography

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Miscellaneous algorithms for density modification

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Automated protein model building combined with iterative structure refinement

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

1 reference

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21 January 2018

Protein structure comparison by alignment of distance matrices

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311833200

21 January 2018

Protein structure alignment by incremental combinatorial extension (CE) of the optimal path

1 reference

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21 January 2018

Replacement of Pro109 by His in TlpA, a thioredoxin-like protein from Bradyrhizobium japonicum, alters its redox properties but not its in vivo functions.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311833200

21 January 2018

A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311833200

21 January 2018

Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria

1 reference

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21 January 2018

Reconstitution of a disulfide isomerization system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311833200

21 January 2018

Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311833200

21 January 2018

Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311833200

21 January 2018

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

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21 January 2018

The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form.

1 reference

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Random circular permutation of DsbA reveals segments that are essential for protein folding and stability

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Structural characterisation and functional significance of transient protein-protein interactions.

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

1 reference

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21 January 2018

Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli

1 reference

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21 January 2018

Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant

1 reference

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Microscopic pKa values of Escherichia coli thioredoxin.

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21 January 2018

Why is DsbA such an oxidizing disulfide catalyst?

1 reference

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Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases

1 reference

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Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization

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Molecular mechanisms of cytochrome c biogenesis: three distinct systems.

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Cytochrome c maturation: a complex pathway for a simple task?

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Genomic analyses of bacterial respiratory and cytochrome c assembly systems: Bordetella as a model for the system II cytochrome c biogenesis pathway

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Accurate bond and angle parameters for X-ray protein structure refinement

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The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly

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

1 reference

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21 January 2018

Oxidative protein folding is driven by the electron transport system

1 reference

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21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M311833200

21 January 2018

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

1 reference

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Oxidation-reduction properties of disulfide-containing proteins of the Rhodobacter capsulatus cytochrome c biogenesis system

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Identifiers

10.1074/JBC.M311833200

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