1kay

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[[Image:1kay.jpg|left|200px]]<br /><applet load="1kay" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kay.jpg|left|200px]]
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caption="1kay, resolution 1.7&Aring;" />
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'''70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71A MUTANT'''<br />
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{{Structure
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|PDB= 1kay |SIZE=350|CAPTION= <scene name='initialview01'>1kay</scene>, resolution 1.7&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71A MUTANT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1KAY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAY OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8663302 8663302]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8663302 8663302]
[[Category: Adenosinetriphosphatase]]
[[Category: Adenosinetriphosphatase]]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:14:54 2008''

Revision as of 10:14, 20 March 2008

Image:1kay.jpg


PDB ID 1kay

Drag the structure with the mouse to rotate
, resolution 1.7Å
Ligands: , , and
Activity: Adenosinetriphosphatase, with EC number 3.6.1.3
Coordinates: save as pdb, mmCIF, xml



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. 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

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