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. 1997 Dec;6(12):2659–2662. doi: 10.1002/pro.5560061222

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

K A Buss 1, C Ingram-Smith 1, J G Ferry 1, D A Sanders 1, M S Hasson 1
PMCID: PMC2143604  PMID: 9416619

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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Selected References

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