Structure of the soluble domain of a membrane-anchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties11Edited by R. Huber

Capitani, Guido; Rossmann, Reinhild; Sargent, David F.; Grütter, Markus G.; Richmond, Timothy J.; Hennecke, Hauke

doi:10.1006/jmbi.2001.4913

Cited by 38 publications

(35 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2A). Similar additions to the thioredoxin fold have been described recently in the structures of Bradyrhizobium japonicum CcmG (59) and TlpA, which is essential for biosynthesis of the cytochrome aa 3 oxidase from B. japonicum (60).…”

Section: High-resolution Structures Of Oxidized and Reduced Resa-supporting

confidence: 72%

Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA

Crow

Acheson

Brun

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

Post-translational maturation of cytochromes c involves the covalent attachment of heme to the Cys-XxxXxx-Cys-His motif of the apo-cytochrome. For this process, the two cysteines of the motif must be in the reduced state. In bacteria, this is achieved by dedicated, membrane-bound thiol-disulfide oxidoreductases with a high reducing power, which are essential components of cytochrome c maturation systems and are also linked to cellular disulfide-bond formation machineries. Here we report high-resolution structures of oxidized and reduced states of a soluble, functional domain of one such oxidoreductase, ResA, from Bacillus subtilis. The structures elucidate the structural basis of the protein's high reducing power and reveal the largest redox-coupled conformational changes observed to date in any thioredoxin-like protein. These redox-coupled changes alter the protein surface and illustrate how the redox state of ResA predetermines to which substrate it binds. Furthermore, a polar cavity, present only in the reduced state, may confer specificity to recognize apo-cytochrome c. The described features of ResA are likely to be general for bacterial cytochrome c maturation systems.

show abstract

Section: High-resolution Structures Of Oxidized and Reduced Resa-supporting

confidence: 72%

Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA

Crow

Acheson

Brun

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Exceptions are the thioredoxin-like proteins anchored to the inner bacterial membrane. As an example, TlpA (thioredoxin-like protein A) from Bradyrhizobium japonicum exhibits a low redox potential (Ϫ259 mV) despite its periplasmic orientation and is required for cytochrome aa 3 maturation (9). However, no high redox potential has ever been reported for cytoplasmic TDOR.…”

mentioning

confidence: 99%

Structural and Mechanistic Insights into Unusual Thiol Disulfide Oxidoreductase

Garcin

Bornet

Elantak

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: TDOR are ubiquitous and catalyze important cell redox reactions. Results: Dtrx presents atypical physicochemical properties and a positive surface around its active site, suggesting a specificity for it(s) substrate(s). Conclusion: Active site histidine plays an important role in the molecular mechanism of Dtrx catalysis. Significance: Structural and functional studies of such atypical systems will give new insights into the TDOR catalytic mechanism.

show abstract

“…Asp26 in TRX has been implicated in deprotonating the second cysteine in the Cys-X-X-Cys motif via a nearby water molecule (4,17). Interestingly, B. japonicum TlpA, a periplasmic TRX-like protein that is required for the maturation of aa 3 -type cytochromes (2,19), contains an acidic residue (Glu78) that aligns with the equivalent residue in CcmG. Therefore, Glu86 in CcmG and Glu78 in TlpA are in a prime position to fulfill a role in catalysis similar to that of Asp26 in TRX.…”

mentioning

confidence: 99%

The Acidic Nature of the CcmG Redox-Active Center Is Important for CytochromecMaturation inEscherichia coli

et al. 2004

View full text Add to dashboard Cite

show abstract

Structure of the soluble domain of a membrane-anchored thioredoxin-like protein from Bradyrhizobium japonicum reveals unusual properties11Edited by R. Huber

Cited by 38 publications

References 53 publications

Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA

Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA

Structural and Mechanistic Insights into Unusual Thiol Disulfide Oxidoreductase

The Acidic Nature of the CcmG Redox-Active Center Is Important for CytochromecMaturation inEscherichia coli

Contact Info

Product

Resources

About