Functional transitions in myosin: Role of highly conserved Gly and Glu residues in the active site

被引：30

作者：

Onishi, H ^{[1
]}

Morales, MF ^{[1
]}

Kojima, S ^{[1
]}

Katoh, K ^{[1
]}

Fujiwara, K ^{[1
]}

机构：

[1] UNIV PACIFIC,SAN FRANCISCO,CA 94115

来源：

BIOCHEMISTRY | 1997年 / 36卷 / 13期

关键词：

D O I：

10.1021/bi9630772

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：

It has been proposed from crystallographic comparisons [Fisher, A. J., Smith, C. A., Thoden, J. B., Smith, R., Sutoh, K., Holden, H. M., & Rayment, I. (1995) Biochemistry 34, 8960-8972] that in one of the important transitions of myosin head (M), M . ATP --> M . ADP . P-i, a rotation occurs in Gly(468) (of chicken smooth muscle myosin). We find that mutation of this Gly to Ala does block the transition. Searching for proton accepters in ATPase catalysis, we also find that mutation of a candidate (Glu(470) of chicken smooth muscle myosin) blocks the transition. Interpretations of both findings are examined.

引用

页码：3767 / 3772

页数：6

共 27 条

[1]

ADELSTEIN RS, 1981, J BIOL CHEM, V256, P7501

[2] MAGNESIUM ION-DEPENDENT ADENOSINE-TRIPHOSPHATASE OF MYOSIN - 2-STEP PROCESSES OF ADENOSINE-TRIPHOSPHATE ASSOCIATION AND ADENOSINE-DIPHOSPHATE DISSOCIATION [J].