Allosteric ACTion: the varied ACT domains regulating enzymes of amino-acid metabolism

被引:64
作者
Lang, Eric J. M. [1 ]
Cross, Penelope J. [1 ]
Mittelstaedt, Gerd [1 ]
Jameson, Geoffrey B. [2 ]
Parker, Emily J. [1 ]
机构
[1] Univ Canterbury, Biomol Interact Ctr, Maurice Wilkins Ctr, Dept Chem, Christchurch 1, New Zealand
[2] Massey Univ, Inst Fundamental Sci, Palmerston North, New Zealand
关键词
CRYSTAL-STRUCTURE; ASPARTATE KINASE; STRUCTURAL BASIS; SYNTHASE; SUBUNIT; INHIBITION; MECHANISM; PROTEINS; MODEL;
D O I
10.1016/j.sbi.2014.10.007
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
Allosteric regulation of enzyme activity plays important metabolic roles. Here we review the allostery of enzymes of amino-acid metabolism conferred by a discrete domain known as the ACT domain. This domain of 60-70 residues has a beta alpha beta beta alpha beta topology leading to a four-stranded beta(4)beta(1)beta(3)beta(2) antiparallel sheet with two antiparallel helices on one face. Extensive sequence variation requires a combined sequence/ structure/function analysis for identification of the ACT domain. Common features include highly varied modes of self-association of ACT domains, ligand binding at domain interfaces, and transmittal of allosteric signals through conformational changes and/or the manipulation of quaternary equilibria. A recent example illustrates the relatively facile adoption of this versatile module of allostery by gene fusion.
引用
收藏
页码:102 / 111
页数:10
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