The crystal structure of Arabidopsis VSP1 reveals the plant class C-like phosphatase structure of the DDDD superfamily of phosphohydrolases.
The crystal structure of Arabidopsis VSP1 reveals the plant class C-like phosphatase structure of the DDDD superfamily of phosphohydrolases.
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拟南芥 VSP1 的晶体结构揭示了磷酸水解酶 DDDD 超家族的植物 C 类磷酸酶结构
DOI：
10.1371/journal.pone.0049421
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发表时间：
2012
期刊：
影响因子：
3.7
通讯作者：
Zhang M
中科院分区：
文献类型：
--
作者：
Chen Y;Wei J;Wang M;Shi Z;Gong W;Zhang M
拟南芥营养贮藏蛋白VSP 1和VSP 2是酸性磷酸酶，属于卤酸脱卤酶（HAD）超家族。除了潜在的营养储存功能外，它们还被认为参与植物防御和花的发育。为了深入了解蛋白质的结构并获得有关其功能的线索，我们测试了它们的底物特异性并解决了VSP 1的结构。这两种酶的酸性磷酸酶活性需要二价金属如镁离子。相反，这两种酶的活性被钒酸盐和磷酸盐抑制，但对无机磷酸盐有抗性。VSP 1和VSP 2对所测试的任何生理底物都没有表现出显著的活性。在目前的研究中，我们提出了重组VSP 1的晶体结构在1.8纳米分辨率通过硒代蛋氨酸单波长异常衍射（SAD）。具体而言，发现α/β核心结构域顶部的α-螺旋帽结构域参与二聚化。此外，尽管VSP 1和其他HAD酶之间的低序列相似性，包含保守的活性位点和催化机制的VSP 1的核心结构域显示了一个经典的卤酸脱卤酶折叠。此外，我们发现VSP 1是区别于细菌C类酸性磷酸酶P4的几个结构特征。据我们所知，这是首次揭示植物营养贮藏蛋白晶体结构的研究。
Arabidopsis thaliana vegetative storage proteins, VSP1 and VSP2, are acid phosphatases and belong to the haloacid dehalogenase (HAD) superfamily. In addition to their potential nutrient storage function, they were thought to be involved in plant defense and flower development. To gain insights into the architecture of the protein and obtain clues about its function, we have tested their substrate specificity and solved the structure of VSP1. The acid phosphatase activities of these two enzymes require divalent metal such as magnesium ion. Conversely, the activity of these two enzymes is inhibited by vanadate and molybdate, but is resistant to inorganic phosphate. Both VSP1 and VSP2 did not exhibit remarkable activities to any physiological substrates tested. In the current study, we presented the crystal structure of recombinant VSP1 at 1.8 Å resolution via the selenomethionine single-wavelength anomalous diffraction (SAD). Specifically, an α-helical cap domain on the top of the α/β core domain is found to be involved in dimerization. In addition, despite of the low sequence similarity between VSP1 and other HAD enzymes, the core domain of VSP1 containing conserved active site and catalytic machinery displays a classic haloacid dehalogenase fold. Furthermore, we found that VSP1 is distinguished from bacterial class C acid phosphatase P4 by several structural features. To our knowledge, this is the first study to reveal the crystal structure of plant vegetative storage proteins.
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DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
影响因子：
2.9
作者：
Felts, Richard L.;Ou, Zhonghui;Tanner, John J.
通讯作者：
Tanner, John J.
影响因子：
7.4
作者：
Penheiter, AR;Duff, SMG;Sarath, G
通讯作者：
Sarath, G
DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL