NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A

Journal of Molecular Biology
K B WongS M Freund

Abstract

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 Barstar C40/82A, a mutant in which the two cysteine residues have been replaced by alanine, has been used as a pseudo wild-type in folding studies and in the crystal structure of the barnase:barstar C40/82A complex.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

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Citations

Nov 25, 1998·Protein Science : a Publication of the Protein Society·Y GaoD P Giedroc
Jul 1, 1999·Protein Science : a Publication of the Protein Society·T R KillickA R Fersht
Jun 15, 2007·BMC Structural Biology·Daniele Dell'OrcoFrancesca Fanelli
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Apr 28, 2020·Journal of the American Chemical Society·Or SzekelyLucio Frydman
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May 17, 2012·The Journal of Physical Chemistry. B·Kazuhiro Takemura, Akio Kitao
Apr 7, 2011·Biochimica Et Biophysica Acta·Michael KovermannJochen Balbach

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