1OT3
Crystal structure of Drosophila deoxyribonucleotide kinase complexed with the substrate deoxythymidine
Summary for 1OT3
| Entry DOI | 10.2210/pdb1ot3/pdb |
| Descriptor | Deoxyribonucleoside Kinase, SULFATE ION, THYMIDINE, ... (4 entities in total) |
| Functional Keywords | protein-deoxynucleoside complex, transferase |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 8 |
| Total formula weight | 235820.43 |
| Authors | Mikkelsen, N.E.,Johansson, K.,Karlsson, A.,Knecht, W.,Andersen, G.,Piskur, J.,Munch-Petersen, B.,Eklund, H. (deposition date: 2003-03-21, release date: 2003-05-27, Last modification date: 2023-10-25) |
| Primary citation | Mikkelsen, N.E.,Johansson, K.,Karlsson, A.,Knecht, W.,Andersen, G.,Piskur, J.,Munch-Petersen, B.,Eklund, H. Structural Basis for Feedback Inhibition of the Deoxyribonucleoside Salvage Pathway: Studies of the Drosophila Deoxyribonucleoside Kinase. Biochemistry, 42:5706-5712, 2003 Cited by PubMed Abstract: Deoxyribonucleoside kinases are feedback inhibited by the final products of the salvage pathway, the deoxyribonucleoside triphosphates. In the present study, the mechanism of feedback inhibition is presented based on the crystal structure of a complex between the fruit fly deoxyribonucleoside kinase and its feedback inhibitor deoxythymidine triphosphate. The inhibitor was found to be bound as a bisubstrate inhibitor with its nucleoside part in the nucleoside binding site and with its phosphate groups partially occupying the phosphate donor site. The overall structure of the enzyme--inhibitor complex is very similar to the enzyme--substrate complexes with deoxythymidine and deoxycytidine, except for a conformational change within a region otherwise directly involved in catalysis. This conformational change involves a magnesium ion, which is coordinated in the inhibitor complex to the phosphates and to the primary base, Glu52, that normally is positioned close to the 5'-OH of the substrate deoxyribose. PubMed: 12741827DOI: 10.1021/bi0340043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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