View source for 1ab7

[[Image:1ab7.gif|left|200px]]

 {{Structure
|PDB= 1ab7 |SIZE=350|CAPTION= <scene name='initialview01'>1ab7</scene>
|SITE= <scene name='pdbsite=BNB:Residue+26+-+44+Is+The+Region+That+Binds+To+The+Active+S+...'>BNB</scene>
|LIGAND= 
|ACTIVITY= 
|GENE= 
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ab7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ab7 OCA], [http://www.ebi.ac.uk/pdbsum/1ab7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ab7 RCSB]</span>
}}

'''NMR 15N RELAXATION AND STRUCTURAL STUDIES REVEAL CONFORMATIONAL EXCHANGE IN BARSTAR C40/82A, 30 STRUCTURES'''


==Overview==
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 Barstar C40/82A, a mutant in which the two cysteine residues have been replaced by alanine, has been used as a pseudo wild-type in folding studies and in the crystal structure of the barnase:barstar C40/82A complex.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.

==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]. 

==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:[http://www.ncbi.nlm.nih.gov/pubmed/9159486 9159486]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Single protein]]
[[Category: Fersht, A R.]]
[[Category: Freund, S M.V.]]
[[Category: Wong, K B.]]
[[Category: ribonuclease inhibitor]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:36:57 2008''