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TitleSynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2156, Year 2023
Publish dateApr 14, 2023
AuthorsLucas Gewehr / Benedikt Junglas / Ruven Jilly / Johannes Franz / Wenyu Eva Zhu / Tobias Weidner / Mischa Bonn / Carsten Sachse / Dirk Schneider /
PubMed AbstractDynamin-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- ...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.
External linksNat Commun / PubMed:37059718 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

14993

7zw6

EMDB-14993, PDB-7zw6:
Oligomeric structure of SynDLP
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • synechocystis sp. pcc 6803 (bacteria)
KeywordsLIPID BINDING PROTEIN / BDLP / cyanobacteria / membrane remodeling

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