The name's bond......disulfide bond.
A repeating theme in the structural biology of disulfide oxidants and isomerases is the extraordinary architectural similarity between functionally related proteins from prokaryotes and eukaryotes. The recently determined structure of full-length yeast protein disulfide isomerase (PDI) reveals a U-shaped molecule with two redox-active sites. It bears a remarkable resemblance to the V-shaped, but dimeric, bacterial disulfide isomerases DsbC and DsbG. Similarly, the much-anticipated structure of the bacterial membrane protein DsbB, the redox partner of DsbA, comprises a flexible redox loop embedded in an antiparallel four-helix bundle. This architecture is similar to that of soluble eukaryotic Ero1p and Erv2p proteins, the redox partners of PDI. Importantly, the DsbB crystal structure is a complex with DsbA, providing our first view of the molecular interactions between these two proteins.
Heras
Begoña
B
Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.
Kurz
Mareike
M
Shouldice
Stephen R
SR
Martin
Jennifer L
JL
D004220:Disulfides / Q000737:chemistry*; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011506:Proteins / Q000737:chemistry
D004220:Disulfides; D011506:Proteins