1btb

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(New page: 200px<br /><applet load="1btb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1btb" /> '''THREE-DIMENSIONAL SOLUTION STRUCTURE AND 13C...)
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'''THREE-DIMENSIONAL SOLUTION STRUCTURE AND 13C ASSIGNMENTS OF BARSTAR USING NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY'''<br />
'''THREE-DIMENSIONAL SOLUTION STRUCTURE AND 13C ASSIGNMENTS OF BARSTAR USING NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1BTB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BTB OCA].
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1BTB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BTB OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bycroft, M.]]
[[Category: Bycroft, M.]]
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[[Category: Fersht, A.R.]]
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[[Category: Fersht, A R.]]
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[[Category: Freund, S.M.V.]]
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[[Category: Freund, S M.V.]]
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[[Category: Lubienski, M.J.]]
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[[Category: Lubienski, M J.]]
[[Category: ribonuclease inhibitor]]
[[Category: ribonuclease inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:54:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:53 2008''

Revision as of 09:58, 21 February 2008


1btb

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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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