2V78

Crystal structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase

Summary for 2V78

• Entry DOI: 10.2210/pdb2v78/pdb
• Related: 2VAR
• Descriptor: FRUCTOKINASE (2 entities in total)
• Functional Keywords: kinase, transferase, pfkb family carbohydrate kinase, 2-keto-3-deoxygluconate kinase
• Biological source: SULFOLOBUS SOLFATARICUS
• Total number of polymer chains: 3
• Total formula weight: 104756.14

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: 2007-07-27, release date: 2007-08-07, 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

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: 19018105
DOI: 10.1107/S0907444908036111

Experimental method

X-RAY DIFFRACTION (2 Å)