Crystal structure and evolution of a prokaryotic glucoamylase

被引：71

作者：

Aleshin, AE

Feng, PH

Honzatko, RB

Reilly, PJ ^{[1
]}

机构：

[1] Iowa State Univ Sci & Technol, Dept Chem Engn, Ames, IA 50011 USA

[2] Iowa State Univ Sci & Technol, Dept Biochem Biophys & Mol Biol, Ames, IA 50011 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2003年 / 327卷 / 01期

关键词：

crystal structure; glucoamylase; glycoaminoglycan lyase; maltose phosphorylase; Thermoanaerobacterium thermosaccharolyticum;

D O I：

10.1016/S0022-2836(03)00084-6

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 first crystal structures of a two-domain, prokaryotic glucoamylase were determined to high resolution from the clostridial species Thermoanaerobacterium thermosaccharolyticum with and without acarbose. The N-terminal domain has 18 antiparallel strands arranged in beta-sheets of a super-beta-sandwich. The C-terminal domain is an (alpha/alpha)(6) barrel, lacking the peripheral subdomain of eukaryotic glucoamylases. Interdomain contacts are common to all prokaryotic Family GH15 proteins. Domains similar to those of prokaryotic glucoamylases in maltose phosphorylases (Family GH65) and glycoaminoglycan lyases (Family PL8) suggest evolution from a common ancestor. Eukaryotic glucoamylases may have evolved from prokaryotic glucoamylases by the substitution of the N-terminal domain with the peripheral subdomain and by the addition of a starch-binding domain. (C) 2003 Elsevier Science Ltd. All rights reserved.

引用

页码：61 / 73

页数：13

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