Structural mechanism of muscle contraction

被引：594

作者：

Geeves, MA ^{[1
]}

Holmes, KC

机构：

[1] Univ Kent, Dept Biosci, Canterbury CT2 7NJ, Kent, England

[2] Max Planck Inst Med Res, D-69120 Heidelberg, Germany

来源：

ANNUAL REVIEW OF BIOCHEMISTRY | 1999年 / 68卷

关键词：

actin; myosin; structure; muscle contraction; swinging cross bridge; molecular mechanism; kinetics; mutations;

D O I：

10.1146/annurev.biochem.68.1.687

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

X-ray crystallography shows the myosin cross-bridge to exist in two conformations, the beginning and end of the "power stroke." A long lever-arm undergoes a 60 degrees to 70 degrees rotation between the two states. This rotation is coupled with changes in the active site (OPEN to CLOSED) and phosphate release. Actin binding mediates the transition from CLOSED to OPEN. Kinetics shows that the binding of myosin to actin is a two-step process which affects ATP and ADP affinity. The structural basis of these effects is not explained by the presently known conformers of myosin. Therefore, other states of the myosin cross-bridge must exist. Moreover, cryoelectronmicroscopy has revealed other angles of the cross-bridge lever arm induced by ADP binding. These structural states are presently being characterized by site-directed mutagenesis coupled with kinetic analysis.

引用

页码：687 / 728

页数：42

共 127 条

[1] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].

ABRAHAMS, JP ;

LESLIE, AGW ;

LUTTER, R ;

WALKER, JE .

NATURE, 1994, 370 (6491) :621-628

[2] ACTOMYOSIN KINETICS AND IN-VITRO MOTILITY OF WILD-TYPE DROSOPHILA ACTIN AND THE EFFECTS OF 2 MUTATIONS IN THE ACT88F GENE [J].

ANSON, M ;

DRUMMOND, DR ;

GEEVES, MA ;

HENNESSEY, ES ;

RITCHIE, MD ;

SPARROW, JC .

BIOPHYSICAL JOURNAL, 1995, 68 (05) :1991-2003

[3] Myosin motors with artificial lever arms [J].

Anson, M ;

Geeves, MA ;

Kurzawa, SE ;

Manstein, DJ .

EMBO JOURNAL, 1996, 15 (22) :6069-6074

[4] OXYGEN-EXCHANGE IN GAMMA-PHOSPHORYL GROUP OF PROTEIN-BOUND ATP DURING MG2+-DEPENDENT ADENOSINE-TRIPHOSPHATASE ACTIVITY OF MYOSIN [J].

BAGSHAW, CR ;

TRENTHAM, DR ;

WOLCOTT, RG ;

BOYER, PD .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1975, 72 (07) :2592-2596

[5] REVERSIBILITY OF ADENOSINE-TRIPHOSPHATE CLEAVAGE BY MYOSIN [J].

BAGSHAW, CR ;

TRENTHAM, DR .

BIOCHEMICAL JOURNAL, 1973, 133 (02) :323-328

[6] Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region [J].

Batra, R ;

Geeves, MA ;

Manstein, DJ .

BIOCHEMISTRY, 1999, 38 (19) :6126-6134

[7] Point mutations in human beta cardiac myosin heavy chain have differential effects on sarcomeric structure and assembly: An ATP binding site change disrupts both thick and thin filaments, whereas hypertrophic cardiomyopathy mutations display normal assembly [J].

Becker, KD ;

Gottshall, KR ;

Hickey, R ;

Perriard, JC ;

Chien, KR .

JOURNAL OF CELL BIOLOGY, 1997, 137 (01) :131-140

[8] Fine tuning a molecular motor: The location of alternative domains in the Drosophila myosin head [J].

Bernstein, SI ;

Milligan, RA .

JOURNAL OF MOLECULAR BIOLOGY, 1997, 271 (01) :1-6

[9] Fifty ways to love your lever: Myosin motors [J].

Block, SM .

CELL, 1996, 87 (02) :151-157

[10] Structural aspects of heterotrimeric G-protein signaling [J].

Bohm, A ;

Gaudet, R ;

Sigler, PB .

CURRENT OPINION IN BIOTECHNOLOGY, 1997, 8 (04) :480-487

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