1FO5
SOLUTION STRUCTURE OF REDUCED MJ0307
Summary for 1FO5
| Entry DOI | 10.2210/pdb1fo5/pdb |
| Descriptor | THIOREDOXIN (1 entity in total) |
| Functional Keywords | disulfide oxidoreductase, thioredoxin fold, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, oxidoreductase |
| Biological source | Methanocaldococcus jannaschii |
| Total number of polymer chains | 1 |
| Total formula weight | 9414.07 |
| Authors | Cave, J.W.,Cho, H.S.,Batchelder, A.M.,Kim, R.,Yokota, H.,Wemmer, D.E.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2000-08-24, release date: 2001-04-11, Last modification date: 2024-05-22) |
| Primary citation | Cave, J.W.,Cho, H.S.,Batchelder, A.M.,Yokota, H.,Kim, R.,Wemmer, D.E. Solution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschii. Protein Sci., 10:384-396, 2001 Cited by PubMed Abstract: 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. PubMed: 11266624DOI: 10.1110/ps.35101 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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