Evolution of the arginase fold and functional diversity

被引：59

作者：

Dowling, D. P. ^{[1
]}

Di Costanzo, L. ^{[1
]}

Gennadios, H. A. ^{[1
]}

Christianson, D. W. ^{[1
]}

机构：

[1] Univ Penn, Dept Chem, Roy & Diana Vagelos Labs, Philadelphia, PA 19104 USA

来源：

CELLULAR AND MOLECULAR LIFE SCIENCES | 2008年 / 65卷 / 13期

关键词：

metalloenzyme; protein structure; enzyme inhibitor; X-ray crystallography; cationic amino acid;

D O I：

10.1007/s00018-008-7554-z

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：

Novel structural superfamilies can be identified among the large number of protein structures deposited in the Protein Data Bank based on conservation of fold in addition to conservation of amino acid sequence. Since sequence diverges more rapidly than fold in protein Evolution, proteins with little or no significant sequence identity are occasionally observed to adopt similar folds, thereby reflecting unanticipated evolutionary relationships. Here, we review the unique alpha/beta fold first observed in the manganese metalloenzyme rat liver arginase, consisting of a parallel eight-stranded beta-sheet surrounded by several helices, and its evolutionary relationship with the zinc-requiring and/or iron-requiring histone deacetylases and acetylpolyamine amidohydrolases. Structural comparisons reveal key features of the core alpha/beta fold that contribute to the divergent metal ion specificity and stoichiometry required for the chemical and biological functions of these enzymes.

引用

页码：2039 / 2055

页数：17

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