T-STATE AND R-STATE IN THE CRYSTALS OF BACTERIAL L-LACTATE DEHYDROGENASE REVEAL THE MECHANISM FOR ALLOSTERIC CONTROL

被引：89

作者：

IWATA, S ^{[1
]}

KAMATA, K ^{[1
]}

YOSHIDA, S ^{[1
]}

MINOWA, T ^{[1
]}

OHTA, T ^{[1
]}

机构：

[1] UNIV TOKYO,DEPT AGR CHEM,BUNKYO KU,TOKYO 113,JAPAN

来源：

NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 03期

关键词：

D O I：

10.1038/nsb0394-176

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：

The crystal structure of L-lactate dehydrogenase from Bifidobacterium longum, determined to 2.5 Angstrom resolution, contains a regular 1:1 complex of F and R-state tetramers. A comparison of these two structures within the same crystal lattice and kinetical characterization of the T-R transition in solution provide an explanation for the molecular mechanism of allosteric activation. Substrate affinity is controlled by helix sliding between subunits which is triggered by the binding of the activator, fructose 1,6-bisphosphate. The proposed mechanism can explain activation by chemical modification and mutagenesis, as well as suggesting why vertebrate counterparts are not allosteric.

引用

页码：176 / 185

页数：10

共 43 条

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