7BTN

Crystal structure of human inorganic pyrophosphatase with metal ions

Summary for 7BTN

• Entry DOI: 10.2210/pdb7btn/pdb
• Descriptor: Inorganic pyrophosphatase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: complex, monomer, hydrolase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 35159.29

Authors

Hu, F.,Huang, Z.,Li, L. (deposition date: 2020-04-02, release date: 2020-10-21, Last modification date: 2023-11-29)

Primary citation

Hu, F.,Huang, Z.,Zheng, S.,Wu, Q.,Chen, Y.,Lin, H.,Huang, W.,Li, L.
Structural and biochemical characterization of inorganic pyrophosphatase from Homo sapiens.
Biochem.Biophys.Res.Commun., 533:1115-1121, 2020

PubMed Abstract: 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 Å and 3.40 Å 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 α-helices and ten β-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.

PubMed: 33036755
DOI: 10.1016/j.bbrc.2020.09.139

Experimental method

X-RAY DIFFRACTION (2.382 Å)