1vrs
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(New page: 200px<br /><applet load="1vrs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vrs, resolution 2.85Å" /> '''Crystal structure of...)
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Revision as of 02:58, 21 November 2007
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Crystal structure of the disulfide-linked complex between the N-terminal and C-terminal domain of the electron transfer catalyst DsbD
Overview
DsbD from Escherichia coli catalyzes the transport of electrons from, cytoplasmic thioredoxin to the periplasmic disulfide isomerase DsbC. DsbD, contains two periplasmically oriented domains at the N- and C-terminus, (nDsbD and cDsbD) that are connected by a central transmembrane (TM), domain. Each domain contains a pair of cysteines that are essential for, catalysis. Here, we show that Cys109 and Cys461 form a transient, interdomain disulfide bond between nDsbD and cDsbD in the reaction cycle, of DsbD. We solved the crystal structure of this catalytic intermediate at, 2.85 A resolution, which revealed large relative domain movements in DsbD, as a consequence of a strong overlap between the surface areas of nDsbD, that interact with DsbC and cDsbD. In addition, we have measured the, kinetics of all functional and nonfunctional disulfide exchange reactions, between redox-active, periplasmic proteins and protein domains from the, oxidative DsbA/B and the reductive DsbC/D pathway. We show that both, pathways are separated by large kinetic barriers for nonfunctional, disulfide exchange between components from different pathways.
About this Structure
1VRS is a Protein complex structure of sequences from Escherichia coli. This structure superseeds the now removed PDB entry 1SE1. Active as Protein-disulfide reductase, with EC number 1.8.1.8 Full crystallographic information is available from OCA.
Reference
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD., Rozhkova A, Stirnimann CU, Frei P, Grauschopf U, Brunisholz R, Grutter MG, Capitani G, Glockshuber R, EMBO J. 2004 Apr 21;23(8):1709-19. Epub 2004 Apr 1. PMID:15057279
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