9EM7

Oligomeric structure of SynDLP in presence of GTP

Summary for 9EM7

• Entry DOI: 10.2210/pdb9em7/pdb
• EMDB information: 15695 19812
• Descriptor: Slr0869 protein (1 entity in total)
• Functional Keywords: bdlp, cyanobacteria, membrane remodeling, gtpase, lipid binding protein
• Biological source: Synechocystis sp. PCC 6803
• Total number of polymer chains: 8
• Total formula weight: 749643.18

Authors

Junglas, B.,Gewehr, L.,Schoennenbeck, P.,Schneider, D.,Sachse, C. (deposition date: 2024-03-07, release date: 2024-09-11)

Primary citation

Junglas, B.,Gewehr, L.,Mernberger, L.,Schonnenbeck, P.,Jilly, R.,Hellmann, N.,Schneider, D.,Sachse, C.
Structural basis for GTPase activity and conformational changes of the bacterial dynamin-like protein SynDLP.
Cell Rep, 43:114657-114657, 2024

PubMed Abstract: 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.

PubMed: 39207903
DOI: 10.1016/j.celrep.2024.114657

Experimental method

ELECTRON MICROSCOPY (3.6 Å)