1W7W
Structure and mutational analysis of a plant mitochondrial nucleoside diphosphate kinase: identification of residues involved in serine phosphorylation and oligomerization.
Summary for 1W7W
| Entry DOI | 10.2210/pdb1w7w/pdb |
| Descriptor | NUCLEOSIDE DIPHOSPHATE KINASE (2 entities in total) |
| Functional Keywords | mitochondrial nucleoside diphosphate kinase, ndpk3, pisum sativum, transferase, kinase |
| Biological source | PISUM SATIVUM (PEA) |
| Total number of polymer chains | 6 |
| Total formula weight | 124334.42 |
| Authors | Johansson, M.,MacKenzie-Hose, A.,Andersson, I.,Knorpp, C. (deposition date: 2004-09-13, release date: 2004-10-22, Last modification date: 2023-12-13) |
| Primary citation | Johansson, M.,Mackenzie-Hose, A.,Andersson, I.,Knorpp, C. Structure and Mutational Analysis of a Plant Mitochondrial Nucleoside Diphosphate Kinase: Identification of Residues Involved in Serine Phosphorylation and Oligomerisation Plant Physiol., 136:3034-, 2004 Cited by PubMed Abstract: We report the first crystal structure of a plant (Pisum sativum L. cv Oregon sugarpod) mitochondrial nucleoside diphosphate kinase. Similar to other eukaryotic nucleoside diphosphate kinases, the plant enzyme is a hexamer; the six monomers in the asymmetric unit are arranged as trimers of dimers. Different functions of the kinase have been correlated with the oligomeric structure and the phosphorylation of Ser residues. We show that the occurrence of Ser autophosphorylation depends on enzymatic activity. The mutation of the strictly conserved Ser-119 to Ala reduced the Ser phosphorylation to about one-half of that observed in wild type with only a modest change of enzyme activity. We also show that mutating another strictly conserved Ser, Ser-69, to Ala reduces the enzyme activity to 6% and 14% of wild-type using dCDP and dTDP as acceptors, respectively. Changes in the oligomerization pattern of the S69A mutant were observed by cross-linking experiments. A reduction in trimer formation and a change in the dimer interaction could be detected with a concomitant increase of tetramers. We conclude that the S69 mutant is involved in the stabilization of the oligomeric state of this plant nucleoside diphosphate kinase. PubMed: 15466238DOI: 10.1104/PP.104.044040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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