1kay
From Proteopedia
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70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71A MUTANT
Overview
It has been proposed that lysine 71 of the bovine 70-kDa heat shock, cognate protein might participate in catalysis of ATP hydrolysis by, stabilizing an H2O molecule or an OH- ion for nucleophilic attack on the, gamma-phosphate of the nucleotide (Flaherty, K. M., Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) J. Biol. Chem. 12899-12907;, Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) J. Biol., Chem. 269, 12893-12898). To test this hypothesis, lysine 71 of the ATPase, fragment 70-kDa heat shock cognate protein has been mutated to glutamic, acid, methionine, and alanine; and the kinetic and structural properties, of the mutant proteins have been determined. All three mutant proteins are, devoid of measurable ATP hydrolysis activity. Crystal structures of the, mutant proteins have been determined to a resolution of 1.7 A; all three, have ATP in the nucleotide binding site. These data identify lysine 71 as, a residue that is essential for chemical hydrolysis of ATP.
About this Structure
1KAY is a Single protein structure of sequence from Bos taurus with MG, CL, K and ATP as ligands. Active as Adenosinetriphosphatase, with EC number 3.6.1.3 Full crystallographic information is available from OCA.
Reference
Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis., O'Brien MC, Flaherty KM, McKay DB, J Biol Chem. 1996 Jul 5;271(27):15874-8. PMID:8663302
Page seeded by OCA on Tue Nov 20 19:00:50 2007
Categories: Adenosinetriphosphatase | Bos taurus | Single protein | Brien, M.C.O. | Flaherty, K.M. | Mckay, D.B. | ATP | CL | K | MG | Atp-binding | Heat shock | Hydrolase
