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2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
Published on: August 6, 2018
Structural and docking studies of a nucleoside diphosphate kinase 1 (CsNDPK1) from tea [Camellia sinensis (L.) O.
Gajjeraman Prabu1, Krishnaraj Thirugnanasambantham, Abul Kalam Azad Mandal
1UPASI-Tea Research Foundation, Nirar Dam B.P.O, Valparai, 642127 Tamil Nadu, India.
Abstract:
Nucleoside diphosphate kinase (NDPK, EC 2.7.4.6) is a housekeeping gene, which functions in the general homeostasis of cellular nucleoside triphosphate (NTP) pools. Among the various NDPK isoforms, cytosolic NDPK1 has been shown to be the main NDPK isoform in plants, accounting for more than 70 % of total NDPK activity in plants. For the first time, a full-length cDNA (697 bp), designated as CsNDPK1 was cloned from tea leaves and consisted of a 448-bp open reading frame (ORF) encoding a 147-amino-acid polypeptide with calculated molecular mass of 16.1 kDa and a pI of 6.3. Homology modeling of CsNDPK1 shows that the presented tea NDPK1 also contains several motifs, binding and catalytic sites which are highly conserved among other NDPKs. Docking studies of CsNDPK1 with its substrates (NTPs) are discussed in detail. In summary, we describe a reliable model of CsNDPK1 that can be used in structure-based protein-protein interaction studies for identifying its potential role in intracellular communication and its physiological significance in tea.
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