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| - | [[Image:1ab7.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ab7| PDB=1ab7 | SCENE= }} | | {{STRUCTURE_1ab7| PDB=1ab7 | SCENE= }} |
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| - | '''NMR 15N RELAXATION AND STRUCTURAL STUDIES REVEAL CONFORMATIONAL EXCHANGE IN BARSTAR C40/82A, 30 STRUCTURES'''
| + | ===NMR 15N RELAXATION AND STRUCTURAL STUDIES REVEAL CONFORMATIONAL EXCHANGE IN BARSTAR C40/82A, 30 STRUCTURES=== |
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| - | ==Overview==
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| - | 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 Barstar C40/82A, a mutant in which the two cysteine residues have been replaced by alanine, has been used as a pseudo wild-type in folding studies and in the crystal structure of the barnase:barstar C40/82A complex.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 (Pro27-Glu32) towards the binding site of barnase facilitate the formation of interface hydrogen bonds and aromatic contacts in the complex. Extreme line broadening and missing signals in 1H-15N correlation spectra indicate substantial conformational exchange for a large subset of residues. 15N relaxation data at two magnetic field strengths, 11.74 T and 14.10 T, were used to estimate exchange contributions and to map the spectral density function at five frequencies: 0, 50, 60, 450 and 540 MHz. Based on these results, model-free calculations with the inclusion of estimated exchange contributions were used to derive order parameters and internal correlation times. The validity of this approach has been investigated with model-free calculations that incorporate longitudinal relaxation rates and heteronuclear 1H-15N NOE data only at 11.74 T and 14.10 T. The relaxation data suggest substantial conformational exchange in regions of barstar C40/82A, including the binding loop, the second and the third helices, and the second and the third strands. Amide proton exchange experiments suggest a stable hydrogen bond network for all helices and sheets except the third helix and the C-terminal of the second and the third strands. The combined results indicate a rigid body movement of the second helix and twisting motions of the beta-sheet of barstar, which might be important for the interaction with barnase.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9159486}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9159486 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9159486}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1AB7 is a [[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=1AB7 OCA]. | + | 1AB7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AB7 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Wong, K B.]] | | [[Category: Wong, K B.]] |
| | [[Category: Ribonuclease inhibitor]] | | [[Category: Ribonuclease inhibitor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:04:05 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:31:26 2008'' |
Revision as of 13:31, 30 June 2008
Template:STRUCTURE 1ab7
NMR 15N RELAXATION AND STRUCTURAL STUDIES REVEAL CONFORMATIONAL EXCHANGE IN BARSTAR C40/82A, 30 STRUCTURES
Template:ABSTRACT PUBMED 9159486
About this Structure
1AB7 is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full experimental information is available from OCA.
Reference
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
Page seeded by OCA on Mon Jun 30 16:31:26 2008
