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@ARTICLE{Anand:296558,
author = {Anand, Roopsee and Eschenburg, Susanne and Reubold, Thomas
F.},
title = {{C}rystal structure of the {GTP}ase domain and the bundle
signalling element of dynamin in the {GDP} state},
journal = {Biochemical and biophysical research communications},
volume = {469},
number = {1},
issn = {0006-291X},
address = {Orlando, Fla.},
publisher = {Academic Press},
reportid = {PUBDB-2016-01538},
pages = {76 - 80},
year = {2016},
abstract = {Dynamin is the prototype of a family of large multi-domain
GTPases. The 100 kDa protein is a key playerin
clathrin-mediated endocytosis, where it cleaves off vesicles
from membranes using the energy fromGTP hydrolysis. We have
solved the high resolution crystal structure of a fusion
protein of the GTPasedomain and the bundle signalling
element (BSE) of dynamin 1 liganded with GDP. The structure
providesa hitherto missing snapshot of the GDP state of the
hydrolytic cycle of dynamin and reveals how theswitch I
region moves away from the active site after GTP hydrolysis
and release of inorganic phosphate.Comparing our structure
of the GDP state with the known structures of the GTP state,
the transition stateand the nucleotide-free state of dynamin
1 we describe the structural changes through the
hydrolyticcycle.},
cin = {DOOR},
ddc = {570},
cid = {I:(DE-H253)HAS-User-20120731},
pnm = {6G3 - PETRA III (POF3-622)},
pid = {G:(DE-HGF)POF3-6G3},
experiment = {EXP:(DE-H253)P-P11-20150101},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000368868000012},
pubmed = {pmid:26612256},
doi = {10.1016/j.bbrc.2015.11.074},
url = {https://bib-pubdb1.desy.de/record/296558},
}