| http://purl.uniprot.org/citations/9799500 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9799500 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9799500 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi981510x"xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi981510x"xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/author | "McKay D.B."xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/author | "McKay D.B."xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/author | "Sousa M.C."xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/author | "Sousa M.C."xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/pages | "15392-15399"xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/pages | "15392-15399"xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/title | "The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change."xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/title | "The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change."xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/volume | "37"xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://purl.uniprot.org/core/volume | "37"xsd:string |
| http://purl.uniprot.org/citations/9799500 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9799500 |
| http://purl.uniprot.org/citations/9799500 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9799500 |
| http://purl.uniprot.org/citations/9799500 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9799500 |
| http://purl.uniprot.org/citations/9799500 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/9799500 |
| http://purl.uniprot.org/uniprot/P19120 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9799500 |
| http://purl.uniprot.org/uniprot/#_P19120-citation-9799500 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/9799500 |