1ab7
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NMR 15N RELAXATION AND STRUCTURAL STUDIES REVEAL CONFORMATIONAL EXCHANGE IN BARSTAR C40/82A, 30 STRUCTURES
OverviewOverview
Barstar an 89-residue protein consisting of four helices and a, three-stranded parallel beta-sheet, is the intracellular inhibitor of the, endoribonuclease barnase. Barstar C40/82A, a mutant in which the two, cysteine residues have been replaced by alanine, has been used as a pseudo, wild-type in folding studies and in the crystal structure of the, barnase:barstar C40/82A complex. We have determined a high resolution, solution structure of barstar C40/82A. The structures of barstar C40/82A, and the wild-type are superimposable. A comparison with the crystal, structure of the barnase:barstar C40/82A complex revealed subtle, differences in the regions involved in the binding of barstar to barnase., Side-chain rotations of residues Asn33, Asp35 and Asp39 and a movement of, the binding loop ... [(full description)]
About this StructureAbout this Structure
1AB7 is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens]. Structure known Active Site: BNB. Full crystallographic information is available from [OCA].
ReferenceReference
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A., Wong KB, Fersht AR, Freund SM, J Mol Biol. 1997 May 2;268(2):494-511. PMID:9159486
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