Structural highlights
Function
TORD_SHEMA Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
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
TorD is the cytoplasmic chaperone involved in the maturation of the molybdoenzyme TorA prior to the translocation of the folded protein into the periplasm. The X-ray structure at 2.4 A resolution of the TorD dimer reveals extreme domain swapping between the two subunits. The all-helical architecture of the globular domains within the intertwined molecular dimer shows no similarity with known protein structures. According to sequence similarities, this new fold probably represents the architecture of the chaperones associated with the bacterial DMSO/TMAO reductases and also that of proteins of yet unknown functions. The occurrence of multiple oligomeric forms and the chaperone activity of both monomeric and dimeric TorD raise questions about the possible biological role of domain swapping in this protein.
A novel protein fold and extreme domain swapping in the dimeric TorD chaperone from Shewanella massilia.,Tranier S, Iobbi-Nivol C, Birck C, Ilbert M, Mortier-Barriere I, Mejean V, Samama JP Structure. 2003 Feb;11(2):165-74. PMID:12575936[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tranier S, Iobbi-Nivol C, Birck C, Ilbert M, Mortier-Barriere I, Mejean V, Samama JP. A novel protein fold and extreme domain swapping in the dimeric TorD chaperone from Shewanella massilia. Structure. 2003 Feb;11(2):165-74. PMID:12575936
