The crystal structure of a hyperthermoactive exopolygalacturonase from Thermotoga maritima reveals a unique tetramer

被引：27

作者：

Pijning, Tjaard ^{[1
]}

van Pouderoyen, Gertie ^{[1
]}

Kluskens, Leon ^{[2
]}

van der Oost, John ^{[2
]}

Dijkstra, Bauke W. ^{[1
]}

机构：

[1] Univ Groningen, Biophys Chem Lab, NL-9747 AG Groningen, Netherlands

[2] Univ Wageningen & Res Ctr, Microbiol Lab, NL-6703 HB Wageningen, Netherlands

来源：

FEBS LETTERS | 2009年 / 583卷 / 22期

关键词：

Exopolygalacturonase; X-ray crystallography; Crystal structure; Oligomerization; Thermostability; ACTIVE-SITE; ENDOPOLYGALACTURONASE-I; ASPERGILLUS-ACULEATUS; SEQUENCE ALIGNMENTS; POLYGALACTURONASE; PROTEIN; FEATURES; CRYSTALLOGRAPHY; MUTAGENESIS; FAMILY-28;

D O I：

10.1016/j.febslet.2009.10.047

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 exopolygalacturonase from Thermotoga maritima is the most thermoactive and thermostable pectinase known to date. Here we present its crystal structure at 2.05 angstrom resolution. High structural homology around the active site allowed us to propose a model for substrate binding, explaining the exo-cleavage activity and specificity for non-methylated saturated galacturonate at the non-reducing end. Furthermore, the structure reveals unique features that contribute to the formation of stable tetramers in solution. Such an oligomerization has not been observed before for polygalacturonases. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：3665 / 3670

页数：6

共 40 条

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