1N1C

Crystal Structure Of The Dimeric TorD Chaperone From Shewanella Massilia

Summary for 1N1C

• Entry DOI: 10.2210/pdb1n1c/pdb
• Descriptor: TorA specific chaperone, 2,3-DIHYDROXY-1,4-DITHIOBUTANE (3 entities in total)
• Functional Keywords: chaperone, tord, 3d-domain swapping
• Biological source: Shewanella massilia
• Cellular location: Cytoplasm (By similarity): O87949
• Total number of polymer chains: 2
• Total formula weight: 49617.15

Authors

Tranier, S.,Iobbi-Nivol, C.,Mortier-Barriere, I.,Birck, C.,Mejean, V.,Samama, J.-P. (deposition date: 2002-10-17, release date: 2003-05-13, Last modification date: 2024-10-30)

Primary citation

Tranier, S.,Iobbi-Nivol, C.,Birck, C.,Ilbert, M.,Mortier-Barriere, I.,Mejean, V.,Samama, J.P.
A Novel Protein Fold and Extreme Domain Swapping in the Dimeric TorD Chaperone from Shewanella massilia
Structure, 11:165-174, 2003

PubMed Abstract: 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.

PubMed: 12575936
DOI: 10.1016/S0969-2126(03)00008-X

Experimental method

X-RAY DIFFRACTION (2.4 Å)