2AYT
The crystal structure of a protein disulfide oxidoreductase from aquifex aeolicus
Summary for 2AYT
| Entry DOI | 10.2210/pdb2ayt/pdb |
| Related | 1A8L |
| Descriptor | glutaredoxin-like protein, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | protein disulfide oxidoreductase, glutaredoxin, thioredoxin fold, oxidoreductase |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 2 |
| Total formula weight | 54033.76 |
| Authors | Pedone, E.,D'Ambrosio, K.,De Simone, G.,Rossi, M.,Pedone, C.,Bartolucci, S. (deposition date: 2005-09-08, release date: 2006-07-18, Last modification date: 2024-11-06) |
| Primary citation | Pedone, E.,D'Ambrosio, K.,De Simone, G.,Rossi, M.,Pedone, C.,Bartolucci, S. Insights on a new PDI-like family: structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus J.Mol.Biol., 356:155-164, 2006 Cited by PubMed Abstract: A potential role in disulfide bond formation in the intracellular proteins of thermophilic organisms has recently been attributed to a new family of protein disulfide isomerase (PDI)-like proteins. Members of this family are characterized by a molecular mass of about 26kDa and by two Trx folds, each comprising a CXXC active site motif. We report on the functional and structural characterization of a new member of this family, which was isolated from the thermophilic bacterium Aquifex aeolicus (AaPDO). Functional studies have revealed the high catalytic efficiency of this enzyme in reducing, oxidizing and isomerizing disulfide bridges. Site-directed mutagenesis experiments have suggested that its two active sites have similar functional properties, i.e. that each of them imparts partial activity to the enzyme. This similarity was confirmed by the analysis of the enzyme crystal structure, which points to similar geometrical parameters and solvent accessibilities for the two active sites. The results demonstrated that AaPDO is the most PDI-like of all prokaryotic proteins so far known. Thus, further experimental studies on this enzyme are likely to provide important information on the eukaryotic homologue. PubMed: 16364362DOI: 10.1016/j.jmb.2005.11.041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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