1N1C

Crystal Structure Of The Dimeric TorD Chaperone From Shewanella Massilia

1N1C の概要

• エントリーDOI: 10.2210/pdb1n1c/pdb
• 分子名称: TorA specific chaperone, 2,3-DIHYDROXY-1,4-DITHIOBUTANE (3 entities in total)
• 機能のキーワード: chaperone, tord, 3d-domain swapping
• 由来する生物種: Shewanella massilia
• 細胞内の位置: Cytoplasm (By similarity): O87949
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49617.15

構造登録者

Tranier, S.,Iobbi-Nivol, C.,Mortier-Barriere, I.,Birck, C.,Mejean, V.,Samama, J.-P. (登録日: 2002-10-17, 公開日: 2003-05-13, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)