Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites

被引：133

作者：

Herzberg, O ^{[1
]}

Chen, CCH ^{[1
]}

Kapadia, G ^{[1
]}

McGuire, M ^{[1
]}

Carroll, LJ ^{[1
]}

Noh, SJ ^{[1
]}

DunawayMariano, D ^{[1
]}

机构：

[1] UNIV MARYLAND, DEPT CHEM & BIOCHEM, COLLEGE PK, MD 20742 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1996年 / 93卷 / 07期

关键词：

D O I：

10.1073/pnas.93.7.2652

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The crystal structure of pyruvate phosphate dikinase, a histidyl multiphosphotransfer enzyme that synthesizes adenosine triphosphate, reveals a three-domain molecule in which the phosphohistidine domain is flanked by the nucleotide and the phosphoenolpyruvate/pyruvate domains, with the two substrate binding sites approximate to 45 Angstrom apart, The modes of substrate binding have been deduced by analogy to D-Ala-D-Ala ligase and to pyruvate kinase. Coupling between the two remote active sites is facilitated by two conformational states of the phosphohistidine domain, While the crystal structure represents the state of interaction with the nucleotide, the second state is achieved by swiveling around two flexible peptide linkers. This dramatic conformational transition brings the phosphocarrier residue in close proximity to phosphoenolpyruvate/pyruvate. The swiveling-domain paradigm provides an effective mechanism for communication in complex multidomain/multiactive site proteins.

引用

页码：2652 / 2657

页数：6

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