TY  - JOUR
AU  - Junglas, Benedikt
AU  - Gewehr, Lucas
AU  - Mernberger, Lara
AU  - Schönnenbeck, Philipp
AU  - Jilly, Ruven
AU  - Hellmann, Nadja
AU  - Schneider, Dirk
AU  - Sachse, Carsten
TI  - Structural basis for GTPase activity and conformational changes of the bacterial dynamin-like protein SynDLP
JO  - Cell reports
VL  - 43
IS  - 9
SN  - 2211-1247
CY  - [New York, NY]
PB  - Elsevier
M1  - FZJ-2024-05334
SP  - 114657 -
PY  - 2024
AB  - SynDLP, a dynamin-like protein (DLP) encoded in the cyanobacterium Synechocystis sp. PCC 6803, has recently been identified to be structurally highly similar to eukaryotic dynamins. To elucidate structural changes during guanosine triphosphate (GTP) hydrolysis, we solved the cryoelectron microscopy (cryo-EM) structures of oligomeric full-length SynDLP after addition of guanosine diphosphate (GDP) at 4.1 Å and GTP at 3.6-Å resolution as well as a GMPPNP-bound dimer structure of a minimal G-domain construct of SynDLP at 3.8-Å resolution. In comparison with what has been seen in the previously resolved apo structure, we found that the G-domain is tilted upward relative to the stalk upon GTP hydrolysis and that the G-domain dimerizes via an additional extended dimerization domain not present in canonical G-domains. When incubated with lipid vesicles, we observed formation of irregular tubular SynDLP assemblies that interact with negatively charged lipids. Here, we provide the structural framework of a series of different functional SynDLP assembly states during GTP turnover.
LB  - PUB:(DE-HGF)16
C6  - 39207903
UR  - <Go to ISI:>//WOS:001316475700001
DO  - DOI:10.1016/j.celrep.2024.114657
UR  - https://juser.fz-juelich.de/record/1030511
ER  -