Structural and biochemical characterization of inorganic pyrophosphatase from Homo sapiens
Structural and biochemical characterization of inorganic pyrophosphatase from Homo sapiens
复制标题
智人无机焦磷酸酶的结构和生化特征
DOI:
10.1016/j.bbrc.2020.09.139
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发表时间:
2020-12-17
影响因子:
3.1
通讯作者:
Li, Lisheng
中科院分区:
文献类型:
--
作者:
Hu, Fen;Huang, Zelong;Li, Lisheng
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.