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Journal of Bacteriology, January 2001, p. 680-686, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.680-686.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases

Kathryn A. Buss,1 David R. Cooper,1 Cheryl Ingram-Smith,2 James G. Ferry,2 David Avram Sanders,1 and Miriam S. Hasson1,*

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907,1 and Department of Biochemistry and Molecular Biology, Eberly College of Science, The Pennsylvania State University, University Park, Pennsylvania 16802-45002

Received 27 September 2000/Accepted 25 October 2000

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.

* Corresponding author. Mailing address: Dept. of Biological Sciences, 1392 Lilly Hall of Life Sciences, Purdue University, West Lafayette, IN 47907-1392. Phone: (765) 496-2928. Fax: (765) 496-1189. E-mail: mhasson{at}bragg.bio.purdue.edu.

Journal of Bacteriology, January 2001, p. 680-686, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.680-686.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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