1G99

AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA

1G99 の概要

• エントリーDOI: 10.2210/pdb1g99/pdb
• 分子名称: ACETATE KINASE, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: alpha/beta; askha (acetate and sugar kinases, hsc70, actin) superfamily; conserved epsilon conformation; two similar domains, transferase
• 由来する生物種: Methanosarcina thermophila
• 細胞内の位置: Cytoplasm : P38502
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89834.50

構造登録者

Buss, K.A.,Cooper, D.R.,Ingram-Smith, C.,Ferry, J.G.,Sanders, D.A.,Hasson, M.S. (登録日: 2000-11-22, 公開日: 2000-12-27, 最終更新日: 2024-02-07)

主引用文献

Buss, K.A.,Cooper, D.R.,Ingram-Smith, C.,Ferry, J.G.,Sanders, D.A.,Hasson, M.S.
Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases.
J.Bacteriol., 183:680-686, 2001

PubMed Abstract: Acetate kinase, an enzyme widely distributed in the Bacteria and Archaea domains, catalyzes the phosphorylation of acetate. We have determined the three-dimensional structure of Methanosarcina thermophila acetate kinase bound to ADP through crystallography. As we previously predicted, acetate kinase contains a core fold that is topologically identical to that of the ADP-binding domains of glycerol kinase, hexokinase, the 70-kDa heat shock cognate (Hsc70), and actin. Numerous charged active-site residues are conserved within acetate kinases, but few are conserved within the phosphotransferase superfamily. The identity of the points of insertion of polypeptide segments into the core fold of the superfamily members indicates that the insertions existed in the common ancestor of the phosphotransferases. Another remarkable shared feature is the unusual, epsilon conformation of the residue that directly precedes a conserved glycine residue (Gly-331 in acetate kinase) that binds the alpha-phosphate of ADP. Structural, biochemical, and geochemical considerations indicate that an acetate kinase may be the ancestral enzyme of the ASKHA (acetate and sugar kinases/Hsc70/actin) superfamily of phosphotransferases.

PubMed: 11133963
DOI: 10.1128/JB.183.2.680-686.2001

実験手法

X-RAY DIFFRACTION (2.5 Å)