2VAR
Crystal structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase complexed with 2-keto-3-deoxygluconate
Summary for 2VAR
Entry DOI | 10.2210/pdb2var/pdb |
Related | 2V78 |
Descriptor | FRUCTOKINASE, 2-KETO-3-DEOXYGLUCONATE, 3-deoxy-alpha-D-erythro-hex-2-ulofuranosonic acid, ... (6 entities in total) |
Functional Keywords | kinase, transferase, sulfolobus solfataricus, pfkb family carbohydrate kinase, 2- keto-3-deoxygluconate kinasekinase, 2- keto-3-deoxygluconate kinase |
Biological source | SULFOLOBUS SOLFATARICUS |
Total number of polymer chains | 3 |
Total formula weight | 108385.24 |
Authors | Potter, J.A.,Theodossis, A.,Kerou, M.,Lamble, H.J.,Bull, S.D.,Hough, D.W.,Danson, M.J.,Taylor, G.L. (deposition date: 2007-09-04, release date: 2007-10-02, Last modification date: 2024-05-08) |
Primary citation | Potter, J.A.,Kerou, M.,Lamble, H.J.,Bull, S.D.,Hough, D.W.,Danson, M.J.,Taylor, G.L. The Structure of Sulfolobus Solfataricus 2-Keto-3-Deoxygluconate Kinase. Acta Crystallogr.,Sect.D, 64:1283-, 2008 Cited by PubMed Abstract: The hyperthermophilic archaeon Sulfolobus solfataricus grows optimally above 353 K and utilizes an unusual promiscuous nonphosphorylative Entner-Doudoroff pathway to metabolize both glucose and galactose. It has been proposed that a part-phosphorylative Entner-Doudoroff pathway occurs in parallel in S. solfataricus, in which the 2-keto-3-deoxygluconate kinase (KDGK) is promiscuous for both glucose and galactose metabolism. Recombinant S. solfataricus KDGK protein was expressed in Escherichia coli, purified and crystallized in 0.1 M sodium acetate pH 4.1 and 1.4 M NaCl. The crystal structure of apo S. solfataricus KDGK was solved by molecular replacement to a resolution of 2.0 A and a ternary complex with 2-keto-3-deoxygluconate (KDGlu) and an ATP analogue was resolved at 2.1 A. The complex suggests that the structural basis for the enzyme's ability to phosphorylate KDGlu and 2-keto-3-deoxygalactonate (KDGal) is derived from a subtle repositioning of residues that are conserved in homologous nonpromiscuous kinases. PubMed: 19018105DOI: 10.1107/S0907444908036111 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
