Structural and biochemical characterization of inorganic pyrophosphatase from Homo sapiens

被引：9

作者：

Hu, Fen ^{[1
]}

Huang, Zelong ^{[1
]}

Zheng, Shuping ^{[2
]}

Wu, Qiong ^{[1
]}

Chen, Yan ^{[1
]}

Lin, Hanbin ^{[3
]}

Huang, Wenyang ^{[3
]}

Li, Lisheng ^{[1
,3
]}

机构：

[1] Fujian Med Univ, Key Lab Gastrointestinal Canc, Sch Basic Med Sci, Minist Educ, Fuzhou, Peoples R China

[2] Fujian Med Univ, Publ Technol Serv Ctr, Fuzhou, Peoples R China

[3] Fujian Med Univ, Sch Basic Med Sci, Dept Biochem & Mol Biol, Fuzhou, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2020年 / 533卷 / 04期

基金：

中国国家自然科学基金;

关键词：

Hu-PPase; Pyrophosphatase; Crystal structure; Cell proliferation; IDENTIFICATION; SPECIFICITY; PPA1; SITE;

D O I：

10.1016/j.bbrc.2020.09.139

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：

Inorganic pyrophosphatase (PPase) plays an essential role in energy conservation and provides energy for many biosynthetic pathways. Here, we present two three-dimensional structures of PPase from Homo sapiens (Hu-PPase) at 2.38 angstrom and 3.40 angstrom in different crystallization conditions. One of the Hu-PPase structures complex of two magnesium metal ions was determined to be a monomer (Hu-PPase-mono) here, while the other one to be a dimer-dimer (Hu-PPase-dd). In each asymmetric unit of Hu-PPase-mono, there are four alpha-helices and ten beta-strands and folds as a barrel structure, and the active site contains two magnesium ions. Like PPases from many species, we found that Hu-PPase was able to undergo self-assembly. To our surprise, disruption of the self-assembly of Hu-PPase did not influence its enzymatic activity or the ability to promote cell growth. Our work uncovered that different structure forms of Hu-PPase and found that the pyrophosphatase activity of Hu-PPase is independent of its self-assembly. (C) 2020 Elsevier Inc. All rights reserved.

引用

页码：1115 / 1121

页数：7

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