Nucleoside triphosphatase

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Function

Nucleoside triphosphatase or nucleoside triphosphate diphosphohydrolase (NTPase) is responsible for degradation of nucleotides to their monophosphate form. NTPase is found in mammals and in pathogenic microbes. In mammals NTPase hs a crucial role in regulation of purinergic signalling by hydrolysis of extracellular nucleotides. The function of NTPase in pathogens is still unknown[1].

Disease

Relevance

Structural highlights

The 3D structure of the complex between NTPase 2 and the ATP analog AMPPNP shows the NTPase structure composed of two domains. The structure contains 7 Cys-Cys bonds one of which located between domain I and II and reaching the diametrically positioned monomer was found by mutational analysis to be responsible for activation. The ATP analog - AMPPNP - is located in a cleft and forms interactions with domain I and domain II[2].


NTPase 2 tetramer complex with AMPPNP and Mg++ ion (green) (PDB code 4a5a)

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3D structures of nucleoside triphosphatase3D structures of nucleoside triphosphatase

Updated on 12-May-2020

ReferencesReferences

  1. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  2. Krug U, Zebisch M, Krauss M, Strater N. Structural insight into the activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolases by disulfide reduction. J Biol Chem. 2011 Nov 30. PMID:22130673 doi:10.1074/jbc.M111.294348

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Michal Harel, Joel L. Sussman, Alexander Berchansky