5WRU

Crystal structure of type I inorganic pyrophosphatase from P falciparum

Summary for 5WRU

• Entry DOI: 10.2210/pdb5wru/pdb
• Related: 5WRT
• Descriptor: Probable inorganic pyrophosphatase, PHOSPHATE ION (2 entities in total)
• Functional Keywords: ppi, ppase, novel interfaces, hydrolase
• Biological source: Plasmodium falciparum
• Total number of polymer chains: 5
• Total formula weight: 228061.19

Authors

Jamwal, A.,Yogavel, M.,Sharma, A. (deposition date: 2016-12-03, release date: 2017-10-11, Last modification date: 2025-09-17)

Primary citation

Jamwal, A.,Yogavel, M.,Abdin, M.Z.,Jain, S.K.,Sharma, A.
Structural and Biochemical Characterization of Apicomplexan Inorganic Pyrophosphatases
Sci Rep, 7:5255-5255, 2017

PubMed Abstract: Inorganic pyrophosphatases (PPase) participate in energy cycling and they are essential for growth and survival of organisms. Here we report extensive structural and functional characterization of soluble PPases from the human parasites Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase). Our results show that PfPPase is a cytosolic enzyme whose gene expression is upregulated during parasite asexual stages. Cambialistic PfPPase actively hydrolyzes linear short chain polyphosphates like PP, polyP and ATP in the presence of Zn. A remarkable new feature of PfPPase is the low complexity asparagine-rich N-terminal region that mediates its dimerization. Deletion of N-region has an unexpected and substantial effect on the stability of PfPPase domain, resulting in aggregation and significant loss of enzyme activity. Significantly, the crystal structures of PfPPase and TgPPase reveal unusual and unprecedented dimeric organizations and provide new fundamental insights into the variety of oligomeric assemblies possible in eukaryotic inorganic PPases.

PubMed: 28701714
DOI: 10.1038/s41598-017-05234-y

Experimental method

X-RAY DIFFRACTION (3.193 Å)