2JAQ
Structure of deoxyadenosine kinase from M. mycoides with bound dCTP
Summary for 2JAQ
| Entry DOI | 10.2210/pdb2jaq/pdb |
| Related | 2JAS 2JAT |
| Descriptor | DEOXYGUANOSINE KINASE, 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | kinase, transferase, deoxyribonucleoside kinase |
| Biological source | MYCOPLASMA MYCOIDES SUBSP. MYCOIDES SC |
| Total number of polymer chains | 2 |
| Total formula weight | 49512.02 |
| Authors | Welin, M.,Wang, L.,Eriksson, S.,Eklund, H. (deposition date: 2006-11-30, release date: 2007-01-03, Last modification date: 2024-05-08) |
| Primary citation | Welin, M.,Wang, L.,Eriksson, S.,Eklund, H. Structure-Function Analysis of a Bacterial Deoxyadenosine Kinase Reveals the Basis for Substrate Specificity. J.Mol.Biol., 366:1615-, 2007 Cited by PubMed Abstract: Deoxyribonucleoside kinases (dNKs) catalyze the transfer of a phosphoryl group from ATP to a deoxyribonucleoside (dN), a key step in DNA precursor synthesis. Recently structural information concerning dNKs has been obtained, but no structure of a bacterial dCK/dGK enzyme is known. Here we report the structure of such an enzyme, represented by deoxyadenosine kinase from Mycoplasma mycoides subsp. mycoides small colony type (Mm-dAK). Superposition of Mm-dAK with its human counterpart's deoxyguanosine kinase (dGK) and deoxycytidine kinase (dCK) reveals that the overall structures are very similar with a few amino acid alterations in the proximity of the active site. To investigate the substrate specificity, Mm-dAK has been crystallized in complex with dATP and dCTP, as well as the products dCMP and dCDP. Both dATP and dCTP bind to the enzyme in a feedback-inhibitory manner with the dN part in the deoxyribonucleoside binding site and the triphosphates in the P-loop. Substrate specificity studies with clinically important nucleoside analogs as well as several phosphate donors were performed. Thus, in this study we combine structural and kinetic data to gain a better understanding of the substrate specificity of the dCK/dGK family of enzymes. The structure of Mm-dAK provides a starting point for making new anti bacterial agents against pathogenic bacteria. PubMed: 17229440DOI: 10.1016/J.JMB.2006.12.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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