Crystallization of acetate kinase from Methanosarcina thermophila and prediction of its fold

Protein Science : a Publication of the Protein Society
K A BussM S Hasson

Abstract

The unique biochemical properties of acetate kinase present a classic conundrum in the study of the mechanism of enzyme-catalyzed phosphoryl transfer. Large, single crystals of acetate kinase from Methanosarcina thermophila were grown from a solution of ammonium sulfate in the presence of ATP. The crystals diffract to beyond 1.7 A resolution. Analysis of X-ray data from the crystals is consistent with a space group of C2 and unit cell dimensions a = 181 A, b = 67 A, c = 83 A, beta = 103 degrees. Diffraction data have been collected from the crystals at 110 and 277 K. Data collected at 277 K extend to lower resolution, but are more reproducible. The orientation of a noncrystallographic two-fold axis of symmetry has been determined. Based on an analysis of the predicted amino acid sequences of acetate kinase from several organisms, we hypothesize that acetate kinase is a member of the sugar kinase/actin/hsp70 structural family.

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Citations

Jul 4, 2002·Journal of Molecular Biology·Sara CheekNick V Grishin
Mar 19, 2005·Journal of Bacteriology·Cheryl Ingram-SmithJames G Ferry
Mar 10, 2005·Microbiology and Molecular Biology Reviews : MMBR·Alan J Wolfe
Mar 19, 2014·PloS One·Siu Hung Joshua ChanPeter Ruhdal Jensen
Jun 30, 2018·Genome Announcements·Lauren E CookRobert P Gunsalus
Mar 17, 1999·FEMS Microbiology Reviews·J G Ferry

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