|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
37
|
|
pubmed:dateCreated |
2005-9-14
|
|
pubmed:abstractText |
Here, we present the 1.9-A crystal structure of the nucleotide-free GTPase domain of dynamin 1 from Rattus norvegicus. The structure corresponds to an extended form of the canonical GTPase fold observed in Ras proteins. Both nucleotide-binding switch motifs are well resolved, adopting conformations that closely resemble a GTP-bound state not previously observed for nucleotide-free GTPases. Two highly conserved arginines, Arg-66 and Arg-67, greatly restrict the mobility of switch I and are ideally positioned to relay information about the nucleotide state to other parts of the protein. Our results support a model in which switch I residue Arg-59 gates GTP binding in an assembly-dependent manner and the GTPase effector domain functions as an assembly-dependent GTPase activating protein in the fashion of RGS-type GAPs.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-10187814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-10206643,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-10559860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-10966476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-10970849,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-11031245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-11208124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-11242086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-11454452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-11689422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-11701921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-12578348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-14502270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-15004222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-15510214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-1569940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-15824135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-1899707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-2476675,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-2529977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-7560005,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-7877693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-7877694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-8101525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-8126598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-8259210,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-8335685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-8903506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-9219684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-9305951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-9338791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-9697416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16141317-9757107
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
13
|
|
pubmed:volume |
102
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
13093-8
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:16141317-Animals,
pubmed-meshheading:16141317-Arginine,
pubmed-meshheading:16141317-Catalysis,
pubmed-meshheading:16141317-Crystallization,
pubmed-meshheading:16141317-Crystallography, X-Ray,
pubmed-meshheading:16141317-Dynamin I,
pubmed-meshheading:16141317-Enzyme Activation,
pubmed-meshheading:16141317-GTP Phosphohydrolases,
pubmed-meshheading:16141317-Guanosine Triphosphate,
pubmed-meshheading:16141317-Kinetics,
pubmed-meshheading:16141317-Mutation,
pubmed-meshheading:16141317-Protein Structure, Tertiary,
pubmed-meshheading:16141317-Rats
|
|
pubmed:year |
2005
|
|
pubmed:articleTitle |
Crystal structure of the GTPase domain of rat dynamin 1.
|
|
pubmed:affiliation |
Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung, Jahnstrasse 29, D-69120 Heidelberg, Germany.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|
