1btb
From Proteopedia
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THREE-DIMENSIONAL SOLUTION STRUCTURE AND 13C ASSIGNMENTS OF BARSTAR USING NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Overview
We present the high-resolution solution structure and 13C assignments of, wild-type barstar, an 89 amino acid residue polypeptide inhibitor of, barnase, derived from heteronuclear NMR techniques. These were obtained, from measurements on unlabeled, uniformly 15N- and 13C/15N-labeled, and, 10% 13C-labeled barstar samples that have both cysteines (at positions 40, and 82) fully reduced. In total, 30 structures were calculated by hybrid, distance geometry-dynamical simulated annealing calculations. The atomic, rms distribution about the mean coordinate positions is 0.42 A for all, backbone atoms and 0.90 A for all atoms. The structure is composed of, three parallel alpha-helices packed against a three-stranded parallel, beta-sheet. A more poorly defined helix links the second beta-strand and, the third major alpha-helix. The loop involved in binding barnase is, extremely well defined and held rigidly by interactions from the main body, of the protein to both ends and the middle of the loop. This structure, will be used to aid protein engineering studies currently taking place on, the free and bound states of barstar and barnase.
About this Structure
1BTB is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.
Reference
Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy., Lubienski MJ, Bycroft M, Freund SM, Fersht AR, Biochemistry. 1994 Aug 2;33(30):8866-77. PMID:8043574
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