Structural highlights
Function
[THIO_METJA] Acts to maintain redox homeostasis; functions as a protein disulfide reductase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The solution structure of the protein disulfide oxidoreductase Mj0307 in the reduced form has been solved by nuclear magnetic resonance. The secondary and tertiary structure of this protein from the archaebacterium Methanococcus jannaschii is similar to the structures that have been solved for the glutaredoxin proteins from Escherichia coli, although Mj0307 also shows features that are characteristic of thioredoxin proteins. Some aspects of Mj0307's unique behavior can be explained by comparing structure-based sequence alignments with mesophilic bacterial and eukaryotic glutaredoxin and thioredoxin proteins. It is proposed that Mj0307, and similar archaebacterial proteins, may be most closely related to the mesophilic bacterial NrdH proteins. Together these proteins may form a unique subgroup within the family of protein disulfide oxidoreductases.
Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii.,Cave JW, Cho HS, Batchelder AM, Yokota H, Kim R, Wemmer DE Protein Sci. 2001 Feb;10(2):384-96. PMID:11266624[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cave JW, Cho HS, Batchelder AM, Yokota H, Kim R, Wemmer DE. Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii. Protein Sci. 2001 Feb;10(2):384-96. PMID:11266624
