Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus(559 views) Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S
Keywords: Crystal Structure, Disulfide Bond, Pdi, Protein Disulfide Oxidoreductase, Thioredoxin Fold, Protein Aapdo, Protein Disulfide Isomerase, Protein Disulfide Reductase (glutathione), Unclassified Drug, Aquifex Aeolicus, Article, Controlled Study, Enzyme Activity, Enzyme Mechanism, Enzyme Structure, Nonhuman, Priority Journal, Protein Analysis, Protein Function, Protein Isolation, Protein Structure, Thermophilic Bacterium, Amino Acid Sequence, Animals, Binding Sites, Cattle, Conserved Sequence, Hydrogen-Ion Concentration, Insulin, Models, Molecular, Molecular Sequence Data, Mutation, Oxidation-Reduction, Protein Disulfide-Isomerase, Tertiary, Sequence Alignment, Sequence Homology, Bacteria (microorganisms), Eukaryota, Prokaryota,
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R., Napoli, Italy
Istituto di Biochimica Delle Proteine, C.N.R., Napoli, Italy
Dipartimento Delle Scienze Biologiche, Università degli Studi di Napoli Federico II, Napoli, Italy
Dipartimento di Biologia Strutturale e Funzionale, Università degli Studi di Napoli Federico II, Napoli, Italy
References: Not available.
Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus
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 26 kDa 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 an prokaryotic proteins so far known. Thus, further experimental studies on this enzyme are likely to provide important information on the eukaryotic homologue. (c) 2005 Elsevier Ltd. All rights reserved.
Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus