Evolution of functional diversity in the cupin superfamily

被引：270

作者：

Dunwell, JM ^{[1
]}

Culham, A ^{[1
]}

Carter, CE ^{[1
]}

Sosa-Aguirre, CR ^{[1
]}

Goodenough, PW ^{[1
]}

机构：

[1] Univ Reading, Sch Plant Sci, Reading RG6 6AS, Berks, England

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2001年 / 26卷 / 12期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1016/S0968-0004(01)01981-8

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 cupin superfamily of proteins is among the most functionally diverse of any described to date. It was named on the basis of the conserved P-barrel fold ('cupa' is the Latin term for a small barrel), and comprises both enzymatic and non-enzymatic members, which have either one or two cupin domains. Within the conserved tertiary structure, the variety of biochemical function is provided by minor variation of the residues in the active site and the identity of the bound metal ion. This review discusses the advantages of this particular scaffold and provides an evolutionary analysis of 18 different subclasses within the cupin superfamily.

引用

页码：740 / 746

页数：7

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