Crystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITE (Q27656012)

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English	Crystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITE	scientific article

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31 January 2020

Crystal structure and biophysical properties of Bacillus subtilis BdbD. An oxidizing thiol:disulfide oxidoreductase containing a novel metal site (English)

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31 January 2020

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crystal structure

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Bacillus subtilis

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based on heuristic

inferred from title

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31 January 2020

Mirja Carlsson Möller

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31 January 2020

Lars Hederstedt

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31 January 2020

Nick E. Le Brun

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31 January 2020

Geoffrey Robert Moore

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Geoffrey R Moore

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31 January 2020

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Allison Lewin

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31 January 2020

Oliver Hecht

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17 June 2009

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31 January 2020

Journal of Biological Chemistry

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31 January 2020

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31 January 2020

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31 January 2020

23719-23733

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31 January 2020

Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue

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Structure and Functional Properties of Bacillus subtilis Endospore Biogenesis Factor StoA

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Effects of substitutions in the CXXC active-site motif of the extracytoplasmic thioredoxin ResA

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20 March 2017

Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding

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20 March 2017

A calcium-gated lid and a large beta-roll sandwich are revealed by the crystal structure of extracellular lipase from Serratia marcescens

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Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor

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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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On the role of the cis-proline residue in the active site of DsbA

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

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The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal

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Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa

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A pathway for disulfide bond formation in vivo

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20 March 2017

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

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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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20 March 2017

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20 March 2017

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20 March 2017

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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20 March 2017

Small revisions to predicted distances around metal sites in proteins

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7 April 2017

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7 April 2017

Thioredoxin--a fold for all reasons

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7 April 2017

DSB proteins and bacterial pathogenicity.

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29 September 2017

Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation.

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29 September 2017

Glutaredoxin systems.

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29 September 2017

Reversible disulfide bond formation of intracellular proteins probed by NMR spectroscopy

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29 September 2017

Crystallographic refinement of ligand complexes

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29 September 2017

Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.

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29 September 2017

Calcium signalling in bacteria

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29 September 2017

Bacillus subtilis StoA Is a thiol-disulfide oxidoreductase important for spore cortex synthesis

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29 September 2017

Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells

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29 September 2017

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

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2 June 2018

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2 June 2018

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21 January 2018

Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria.

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21 January 2018

The bdbDC operon of Bacillus subtilis encodes thiol-disulfide oxidoreductases required for competence development

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21 January 2018

Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis.

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21 January 2018

PROCHECK: a program to check the stereochemical quality of protein structures

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21 January 2018

A thioreduction pathway tethered to the membrane for periplasmic cytochromes c biogenesis; in vitro and in vivo studies.

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21 January 2018

Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation.

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21 January 2018

The CXXC motif: a rheostat in the active site.

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21 January 2018

Why is DsbA such an oxidizing disulfide catalyst?

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21 January 2018

Prediction of pKa and redox properties in the thioredoxin superfamily.

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21 January 2018

Structural basis and kinetics of DsbD-dependent cytochrome c maturation

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21 January 2018

Snapshots of DsbA in action: detection of proteins in the process of oxidative folding

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

General Acid/Base Catalysis in the Active Site ofEscherichia coliThioredoxin†

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21 January 2018

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21 January 2018

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Calcium signalling in bacteria

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https://pubmed.ncbi.nlm.nih.gov/19535335

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Oxidative protein folding is driven by the electron transport system

1 reference

https://pubmed.ncbi.nlm.nih.gov/19535335

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A single dipeptide sequence modulates the redox properties of a whole enzyme family

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M109.005785

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19535335%20AND%20SRC:MED&resulttype=core&format=json

31 January 2020

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Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19535335%20AND%20SRC:MED&resulttype=core&format=json

31 January 2020

PubMed publication ID

1 reference

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PMC publication ID

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31 January 2020

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