Abstract

It has been recently shown by differential scanning calorimetry (DSC) that the formation of stable complexes of myosin subfragment 1 (S1) with Mg-ADP and orthovanadate (Vi) or beryllium fluoride (BeFx) causes a global conformational change in the S1 molecule which is reflected in a pronounced increase of S1 thermal stability and in a significant change of S1 domain structure [Shriver, J. W., & Kamath U. (1990) Biochemistry 29, 2556-2564; Levitsky, D. I., Shnyrov, V. L., Khvorov, N. V., Bukatina, A. E., Vedenkina, N. S., Permyakov, E. A., Nikolaeva, O. P., & Poglazov, B. F. (1992) Eur. J. Biochem. 209, 829-835; Bobkov, A. A., Khvorov, N. V., Golitsina, N. L., & Levitsky, D. I. (1993) FEBS Lett. 332, 64-66]. In this work, which continues the previous investigations, we report on a DSC study of the complexes of S1 with various nucleoside diphosphates (NDP). In the absence of Vi or BeFx the various Mg(2+)-NDP and Mg(2+)-PPi had a similar effect on the S1 conformation. All of them had practically no influence on the temperature of the thermal transition but increased its sharpness. However, in the presence of Vi or BeFx the effects of Mg(2+)-NDP complexes were quite different from each other and strongly depended on the base structure of NDP; their effectiveness in inducing conformational changes in S1 and the stability of these complexes decreased in the following order: ADP > CDP > UDP > IDP > GDP.(ABSTRACT TRUNCATED AT 250 WORDS) Study holds ProTherm entries: 5139 Extra Details: global conformational change; domain structure; sharpness;,intermediates

Submission Details

ID: jiLdhRY5

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:28 p.m.

Version: 1

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