期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 65, 期 13, 页码 2039-2055出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-008-7554-z
关键词
metalloenzyme; protein structure; enzyme inhibitor; X-ray crystallography; cationic amino acid
资金
- NIGMS NIH HHS [GM 49758, R01 GM049758-15, R01 GM049758-14, R01 GM049758] Funding Source: Medline
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据