1gr7
From Proteopedia
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CRYSTAL STRUCTURE OF THE DOUBLE MUTANT CYS3SER/SER100PRO FROM PSEUDOMONAS AERUGINOSA AT 1.8 A RESOLUTION
Overview
Azurin is a cupredoxin, which functions as an electron carrier. Its fold, is dominated by a beta-sheet structure. In the present study, azurin, serves as a model system to investigate the importance of a conserved, disulphide bond for protein stability and folding/unfolding. For this, purpose, we have examined two azurin mutants, the single mutant Cys3Ser, which disrupts azurin's conserved disulphide bond, and the double mutant, Cys3Ser/Ser100Pro, which contains an additional mutation at a site distant, from the conserved disulphide. The crystal structure of the azurin double, mutant has been determined to 1.8 A resolution(2), with a crystallographic, R-factor of 17.5% (R(free)=20.8%). A comparison with the wild-type, structure reveals that structural differences are limited to the sites ... [(full description)]
About this Structure
1GR7 is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with CU as [ligand]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the double azurin mutant Cys3Ser/Ser100Pro from Pseudomonas aeruginosa at 1.8 A resolution: its folding-unfolding energy and unfolding kinetics., Okvist M, Bonander N, Sandberg A, Karlsson BG, Krengel U, Xue Y, Sjolin L, Biochim Biophys Acta. 2002 Apr 29;1596(2):336-45. PMID:12007613
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