Stability, catalytic versatility and evolution of the (βα)8-barrel fold

被引：75

作者：

Höcker, B

Jürgens, C

Wilmanns, M

Sterner, R

机构：

[1] Univ Cologne, Inst Biochem, D-50674 Cologne, Germany

[2] DESY, European Mol Biol Lab, Hamburg Outstn, D-22603 Hamburg, Germany

来源：

CURRENT OPINION IN BIOTECHNOLOGY | 2001年 / 12卷 / 04期

关键词：

D O I：

10.1016/S0958-1669(00)00230-5

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The (beta alpha)(8)-barrel is a versatile single-domain protein fold that is adopted by a large number of enzymes. The (beta alpha)(8)-barrel fold has been used as a model to elucidate the structural basis of protein thermostability and in studies to interconvert catalytic activities or substrate specificities by rational design or directed evolution. Recently, the (beta alpha)(4)-half-barrel was identified as a possible structural subdomain.

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页码：376 / 381

页数：6

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