1rxi
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(New page: 200px<br /><applet load="1rxi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rxi, resolution 1.5Å" /> '''pI258 arsenate reduct...)
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Revision as of 23:48, 20 November 2007
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pI258 arsenate reductase (ArsC) triple mutant C10S/C15A/C82S
Overview
Structural insights into formation of the complex between the ubiquitous, thiol-disulfide oxidoreductase thioredoxin and its oxidized substrate are, under-documented owing to its entropical instability. In vitro, it is, possible via a reaction with 5,5'-dithiobis-(2-nitrobenzoic acid) to make, a stable mixed-disulfide complex between thioredoxin from Staphylococcus, aureus and one of its substrates, oxidized pI258 arsenate reductase (ArsC), from S. aureus. In the absence of the crystal structure of an, ArsC-thioredoxin complex, the structures of two precursors of the complex, the ArsC triple mutant ArsC C10SC15AC82S and its 5-thio-2-nitrobenzoic, acid (TNB) adduct, were determined. The ArsC triple mutant has a structure, very similar to that of the reduced form of wild-type ArsC, with a folded, redox helix and a buried catalytic Cys89. In the adduct form, the TNB, molecule is buried in a hydrophobic pocket and the disulfide bridge, between TNB and Cys89 is sterically inaccessible to thioredoxin. In order, to form a mixed disulfide between ArsC and thioredoxin, a change in the, orientation of the TNB-Cys89 disulfide in the structure is necessary.
About this Structure
1RXI is a Single protein structure of sequence from Staphylococcus aureus with K, LCP and CL as ligands. Active as Arsenate reductase (glutaredoxin), with EC number 1.20.4.1 Full crystallographic information is available from OCA.
Reference
The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct., Messens J, Van Molle I, Vanhaesebrouck P, Van Belle K, Wahni K, Martins JC, Wyns L, Loris R, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1180-4. Epub 2004, May 21. PMID:15159594
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