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The name's bond......disulfide bond.

作者信息

Heras Begoña, Kurz Mareike, Shouldice Stephen R, Martin Jennifer L

机构信息

Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.

出版信息

Curr Opin Struct Biol. 2007 Dec;17(6):691-8. doi: 10.1016/j.sbi.2007.08.009. Epub 2007 Oct 22.

Abstract

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.

摘要

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