1kay
From Proteopedia
(New page: 200px<br /><applet load="1kay" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kay, resolution 1.7Å" /> '''70KD HEAT SHOCK COGNA...) |
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| - | [[Image:1kay.jpg|left|200px]]<br /><applet load="1kay" size=" | + | [[Image:1kay.jpg|left|200px]]<br /><applet load="1kay" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kay, resolution 1.7Å" /> | caption="1kay, resolution 1.7Å" /> | ||
'''70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71A MUTANT'''<br /> | '''70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71A MUTANT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | It has been proposed that lysine 71 of the bovine 70-kDa heat shock | + | 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== | ==About this Structure== | ||
| - | 1KAY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, CL, K and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosinetriphosphatase Adenosinetriphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.3 3.6.1.3] Full crystallographic information is available from [http:// | + | 1KAY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosinetriphosphatase Adenosinetriphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.3 3.6.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brien, M | + | [[Category: Brien, M C.O.]] |
| - | [[Category: Flaherty, K | + | [[Category: Flaherty, K M.]] |
| - | [[Category: Mckay, D | + | [[Category: Mckay, D B.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:01 2008'' |
Revision as of 11:32, 21 February 2008
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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 , , and 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 Thu Feb 21 13:32:01 2008
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
