Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction.

Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction. Research Abstract Details 

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Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction. Abstract Text:

S Maruta,K Homma,

Myosin has three highly-conserved, unique loops [B (320-327), M (677-689), and N (127-136)] at the entrance of the ATP binding cleft, and we previously showed that the effects of actin are mediated by a conformational change in loop M [Maruta and Homma (1998) J. Biochem. 124, 528-533]. In the present study, loops M and N were photolabeled respectively with fluorescent probes Mant-8-N(3)-ADP and Mant-2-N(3)-ADP in order to study conformational changes in the loops related to energy transduction. The effect of actin on the conformation of loop N was examined by analyzing fluorescence polarization and acrylamide quenching; the results were then compared with those previously reported for loop M. In contrast to loop M, the fluorescence polarization and the value of K(sv) of the Mant-groups crosslinked to loop N were slightly affected by actin binding. To study conformational changes in loops M and N during the ATPase cycle, FRET was analyzed using TNP-ADP.BeFn and TNP-ADP. AlF(4)(-) as FRET acceptors of Mant fluorescence. The resultant estimated distances between loop M and the active site differed for the Mant-S1.TNP-ADP.BeFn and Mant-S1.TNP-ADP.AlF(4)(-) complexes, whereas the distances between loop N and the active site differed slightly. These findings indicate that the conformation of loop M changes during the ATPase cycle, suggesting that Loop M acts as a signal transducer mediating communication between the ATP- and actin-binding sites. Loop N, by contrast, is not significantly flexible.

Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction. Publishing Authors By Initials

S Maruta,K Homma,

For similar investigative techniques: chemistry, analytical: photometry: spectrophotometry research abstracts see: investigative techniques: chemistry, analytical: photometry: spectrophotometry research

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Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 128

Page Numbers: 695-704

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 2000

Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction. Keywords Mesh Terms:

KEYWORDS: Spectrophotometry

MESH TERMS: metabolism

Chemical & Substance for Abstract: Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Conformational changes in the unique loops bordering the ATP binding cleft of skeletal muscle myosin mediate energy transduction.

AFFILIATION: Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan. shinsaku@t.soka.ac.jp

Country: JAPAN

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MEDLINETA: J Biochem

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