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X-Ray structure of glycerol kinase complexed with an ATP analog implies a novel mechanism for the ATP-dependent glycerol phosphorylation by glycerol kinase



X-Ray structure of glycerol kinase complexed with an ATP analog implies a novel mechanism for the ATP-dependent glycerol phosphorylation by glycerol kinase



Biochemical and Biophysical Research Communications 259(3): 640-644



Glycerol kinase (GK) catalyzes the Mg-ATP-dependent phosphorylation of glycerol which yields glycerol 3-phosphate. The 2.8 ANG new crystal structure of GK complexed with an ATP analog revealed an unexpected position of the gamma-phosphoryl group, which was 7.2 ANG distant from the 3-hydroxyl group of glycerol, 5.5 ANG away from the 3-phosphate of the product (glycerol 3-phosphate) and is stabilized by a beta-hairpin structure. Based on the presented crystal structure and the previously determined structures of GK product complexes, we propose a 3-D model of a nucleophilic inline transfer mechanism for the ATP-dependent phosphorylation of glycerol by GK.

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Accession: 011657077

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PMID: 10364471

DOI: 10.1006/bbrc.1999.0816


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