| http://purl.uniprot.org/citations/20428113 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20428113 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20428113 | http://www.w3.org/2000/01/rdf-schema#comment | "Dynamin is an atypical GTPase that catalyses membrane fission during clathrin-mediated endocytosis. The mechanisms of dynamin's basal and assembly-stimulated GTP hydrolysis are unknown, though both are indirectly influenced by the GTPase effector domain (GED). Here we present the 2.0 A resolution crystal structure of a human dynamin 1-derived minimal GTPase-GED fusion protein, which was dimeric in the presence of the transition state mimic GDP.AlF(4)(-).The structure reveals dynamin's catalytic machinery and explains how assembly-stimulated GTP hydrolysis is achieved through G domain dimerization. A sodium ion present in the active site suggests that dynamin uses a cation to compensate for the developing negative charge in the transition state in the absence of an arginine finger. Structural comparison to the rat dynamin G domain reveals key conformational changes that promote G domain dimerization and stimulated hydrolysis. The structure of the GTPase-GED fusion protein dimer provides insight into the mechanisms underlying dynamin-catalysed membrane fission."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature09032"xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature09032"xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Dyda F."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Dyda F."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Chappie J.S."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Chappie J.S."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Schmid S.L."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Schmid S.L."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Leonard M."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Leonard M."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Acharya S."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/author | "Acharya S."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/pages | "435-440"xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/pages | "435-440"xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/title | "G domain dimerization controls dynamin's assembly-stimulated GTPase activity."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/title | "G domain dimerization controls dynamin's assembly-stimulated GTPase activity."xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/volume | "465"xsd:string |
| http://purl.uniprot.org/citations/20428113 | http://purl.uniprot.org/core/volume | "465"xsd:string |