1kaz: Difference between revisions

Revision as of 10:03, 2 July 2008

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File:1kaz.png

Template:STRUCTURE 1kaz

70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71E MUTANT70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71E MUTANT

Template:ABSTRACT PUBMED 8663302

About this StructureAbout this Structure

1KAZ is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

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 Wed Jul 2 10:03:32 2008

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-'''70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71E MUTANT'''
+===70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71E 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8663302}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_8663302}}
 ==About this Structure==
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 [[Category: Heat shock]]
 [[Category: Hydrolase]]
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