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| http://purl.uniprot.org/citations/10531353 | http://www.w3.org/2000/01/rdf-schema#comment | "To study the relationship between conventional kinesin's structure and function, we identified 13 lethal mutations in the Drosophila kinesin heavy chain motor domain and tested a subset for effects on mechanochemistry. S246F is a moderate mutation that occurs in loop 11 between the ATP- and microtubule-binding sites. While ATP and microtubule binding appear normal, there is a 3-fold decrease in the rate of ATP turnover. This is consistent with the hypothesis that loop 11 provides a structural link that is important for the activation of ATP turnover by microtubule binding. T291M is a severe mutation that occurs in alpha-helix 5 near the center of the microtubule-binding surface. It impairs the microtubule-kinesin interaction and directly effects the ATP-binding pocket, allowing an increase in ATP turnover in the absence of microtubules. The T291M mutation may mimic the structure of a microtubule-bound, partially activated state. E164K is a moderate mutation that occurs at the beta-sheet 5a/loop 8b junction, remote from the ATP pocket. Surprisingly, it causes both tighter ATP-binding and a 2-fold decrease in ATP turnover. We propose that E164 forms an ionic bridge with alpha-helix 5 and speculate that it helps coordinate the alternating site catalysis of dimerized kinesin heavy chain motor domains."xsd:string |
| http://purl.uniprot.org/citations/10531353 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.44.31506"xsd:string |
| http://purl.uniprot.org/citations/10531353 | http://purl.uniprot.org/core/author | "Rose D.J."xsd:string |
| http://purl.uniprot.org/citations/10531353 | http://purl.uniprot.org/core/author | "Saxton W.M."xsd:string |
| http://purl.uniprot.org/citations/10531353 | http://purl.uniprot.org/core/author | "Gilbert S.P."xsd:string |
| http://purl.uniprot.org/citations/10531353 | http://purl.uniprot.org/core/author | "Brendza K.M."xsd:string |
| http://purl.uniprot.org/citations/10531353 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10531353 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/10531353 | http://purl.uniprot.org/core/pages | "31506-31514"xsd:string |
| http://purl.uniprot.org/citations/10531353 | http://purl.uniprot.org/core/title | "Lethal kinesin mutations reveal amino acids important for ATPase activation and structural coupling."xsd:string |
| http://purl.uniprot.org/citations/10531353 | http://purl.uniprot.org/core/volume | "274"xsd:string |
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