Conformations of myosin subfragment 1 ATPase intermediates from neutron and X-ray scattering

Journal of Molecular Biology
R A MendelsonD B Stone

Abstract

In order to elucidate the structural changes that occur during the hydrolysis of ATP by myosin, low-angle neutron and X-ray scattering have been used to investigate the shape of the myosin head (S1) with various bound nucleotides and nucleotide analogs. It was found that the radius of gyration (Rg) of S1.MgADP.AlF4 and of S1MgADP.Vi were similar and significantly smaller (approximately 3%) than the similar Rg values of nucleotide-free S1, S1.MgADP and S1.MgADP.BeFx. In addition, S1 in the presence of MgATP, which is predominantly in the S1.MgADP.Pi state under the experimental conditions employed, showed a change in Rg comparable with that of S1.MgADP.AlF4 and S1.MgADP.Vi. The results obtained here with BeFx and AlF4 are in close harmony with crystallographic results on truncated S1 bearing MgADP.BeFx and MgADP.AlF4. A. Fisher and co-workers have postulated that these two systems, which exhibit some structural differences, represent the pre-hydrolysis state and the transition state of ATP hydrolysis, respectively. It was postulated that this structural difference might alter the orientation of the light-chain-binding domain (tail) of intact S1 relative to the remainder of the molecule. Since this orientation is the major determ...Continue Reading

Citations

Sep 2, 1997·Proceedings of the National Academy of Sciences of the United States of America·T P BurghardtK Ajtai
Aug 5, 1997·Proceedings of the National Academy of Sciences of the United States of America·R Mendelson, E P Morris
Apr 23, 1999·Biochemistry·D B StoneR A Mendelson
Apr 15, 2000·Journal of Molecular Biology·G OfferR Padrón
Dec 1, 1996·Current Opinion in Structural Biology·K C Holmes
Aug 6, 1999·Biochemistry·S Highsmith
Mar 18, 1997·Biochemistry·S ParkT P Burghardt
May 20, 1998·Biophysical Journal·E Burmeister GetzP R Selvin

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