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5IOL

Crystal structure of Nucleoside Diphosphate Kinase from Schistosoma mansoni

Summary for 5IOL
Entry DOI10.2210/pdb5iol/pdb
Related5IOM
DescriptorNucleoside diphosphate kinase (2 entities in total)
Functional Keywordsnucleoside diphosphate kinase, enzyme, transferase
Biological sourceSchistosoma mansoni (Blood fluke)
Total number of polymer chains12
Total formula weight202744.31
Authors
Torini, J.R.S.,Romanello, L.,Bird, L.E.,Nettleship, J.E.,Owens, R.J.,Aller, P.,DeMarco, R.,Brandao-Neto, J.,Pereira, H.M. (deposition date: 2016-03-08, release date: 2017-03-08, Last modification date: 2023-09-27)
Primary citationTorini, J.R.,de Freitas Fernandes, A.,Balasco Serrao, V.H.,Romanello, L.,Bird, L.E.,Nettleship, J.E.,Owens, R.J.,Brandao-Neto, J.,Zeraik, A.E.,DeMarco, R.,D'Muniz Pereira, H.
Characterization of a Schistosoma mansoni NDPK expressed in sexual and digestive organs.
Mol.Biochem.Parasitol., :111187-111187, 2019
Cited by
PubMed Abstract: Nucleoside diphosphate kinases (NDPKs) are crucial to keep the high triphosphate nucleotide levels in the biological process. The enzymatic mechanism has been extensively described; however, the structural characteristics and kinetic parameters have never been fully determined. In Schistosoma mansoni, NDPK (SmNDPK) is directly involved in the pyrimidine and purine salvage pathways, being essential for nucleotide metabolism. The SmNDPK enzymatic activity is the highest of the known purine metabolisms when compared to the mammalian NDPKs, suggesting the importance of this enzyme in the worm metabolism. Here, we report the recombinant expression of SmNDPK that resulted in 1.7 and 1.9 Å apo-form structure in different space-groups, as well as the 2.1 Å SmNDPK.ADP complex. The binding and kinetic assays reveal the ATP-dependence for enzyme activation. Moreover, in situ hybridization showed that SmNDPK transcripts are found in reproductive organs and in the esophagus gland of adult worms, which can be intrinsically related with the oviposition and digestive processes. These results will help us fully understand the crucial participation of this enzyme in Schistosoma mansoni and its importance for the pathology of the disease.
PubMed: 31103556
DOI: 10.1016/j.molbiopara.2019.111187
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.741 Å)
Structure validation

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