2bup: Difference between revisions
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|PDB= 2bup |SIZE=350|CAPTION= <scene name='initialview01'>2bup</scene>, resolution 1.70Å | |PDB= 2bup |SIZE=350|CAPTION= <scene name='initialview01'>2bup</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bup OCA], [http://www.ebi.ac.uk/pdbsum/2bup PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bup RCSB]</span> | |||
}} | }} | ||
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[[Category: Mckay, D B.]] | [[Category: Mckay, D B.]] | ||
[[Category: Sousa, M C.]] | [[Category: Sousa, M C.]] | ||
[[Category: atpase]] | [[Category: atpase]] | ||
[[Category: hydrolase (acting on acid anhydrides)]] | [[Category: hydrolase (acting on acid anhydrides)]] | ||
[[Category: molecular chaperone]] | [[Category: molecular chaperone]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:12:02 2008'' | ||
Revision as of 02:12, 31 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
T13G MUTANT OF THE ATPASE FRAGMENT OF BOVINE HSC70
OverviewOverview
The mechanism by which ATP binding transduces a conformational change in 70-kDa heat shock proteins that results in release of bound peptides remains obscure. Wei and Hendershot demonstrated that mutating Thr37 of hamster BiP to glycine impeded the ATP-induced conformational change, as monitored by proteolysis [(1995) J. Biol. Chem. 270, 26670-26676]. We have mutated the equivalent resitude of the bovine heat shock cognate protein (Hsc70), Thr13, to serine, valine, and glycine. Solution small-angle X-ray scattering experiments on a 60-kDa fragment of Hsc70 show that ATP binding induces a conformational change in the T13S mutant but not the T13V or T13G mutants. The kinetics of ATP-induced tryptophan fluorescence intensity changes in the 60-kDa proteins is biphasic for the T13S mutant but monophasic for T13V or T13G, consistent with a conformational change following initial ATP binding in the T13S mutant but not the other two. Crystallographic structures of the ATPase fragments of the T13S and T13G mutants at 1.7 A resolution show that the mutations do not disrupt the ATP binding site and that the serine hydroxyl mimics the threonine hydroxyl in the wild-type structure. We conclude that the hydroxyl of Thr13 is essential for coupling ATP binding to a conformational change in Hsc70. Molecular modeling suggests this may result from the threonine hydroxyl hydrogen-bonding to a gamma-phosphate oxygen of ATP, thereby inducing a structural shift within the ATPase domain that couples to its interactions with the peptide binding domain.
About this StructureAbout this Structure
2BUP is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change., Sousa MC, McKay DB, Biochemistry. 1998 Nov 3;37(44):15392-9. PMID:9799500
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