7ZW6

Oligomeric structure of SynDLP

Summary for 7ZW6

• Entry DOI: 10.2210/pdb7zw6/pdb
• EMDB information: 14993
• Descriptor: Slr0869 protein (1 entity in total)
• Functional Keywords: bdlp, cyanobacteria, membrane remodeling, lipid binding protein
• Biological source: Synechocystis sp. PCC 6803
• Total number of polymer chains: 8
• Total formula weight: 749643.18

Authors

Gewehr, L.,Junglas, B.,Jilly, R.,Franz, J.,Wenyu, E.Z.,Weidner, T.,Bonn, M.,Sachse, C.,Schneider, D. (deposition date: 2022-05-18, release date: 2023-04-19, Last modification date: 2024-10-23)

Primary citation

Gewehr, L.,Junglas, B.,Jilly, R.,Franz, J.,Zhu, W.E.,Weidner, T.,Bonn, M.,Sachse, C.,Schneider, D.
SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features.
Nat Commun, 14:2156-2156, 2023

PubMed Abstract: Dynamin-like proteins are membrane remodeling GTPases with well-understood functions in eukaryotic cells. However, bacterial dynamin-like proteins are still poorly investigated. SynDLP, the dynamin-like protein of the cyanobacterium Synechocystis sp. PCC 6803, forms ordered oligomers in solution. The 3.7 Å resolution cryo-EM structure of SynDLP oligomers reveals the presence of oligomeric stalk interfaces typical for eukaryotic dynamin-like proteins. The bundle signaling element domain shows distinct features, such as an intramolecular disulfide bridge that affects the GTPase activity, or an expanded intermolecular interface with the GTPase domain. In addition to typical GD-GD contacts, such atypical GTPase domain interfaces might be a GTPase activity regulating tool in oligomerized SynDLP. Furthermore, we show that SynDLP interacts with and intercalates into membranes containing negatively charged thylakoid membrane lipids independent of nucleotides. The structural characteristics of SynDLP oligomers suggest it to be the closest known bacterial ancestor of eukaryotic dynamin.

PubMed: 37059718
DOI: 10.1038/s41467-023-37746-9

Experimental method

ELECTRON MICROSCOPY (3.7 Å)