7ZW6

Oligomeric structure of SynDLP

7ZW6 の概要

• エントリーDOI: 10.2210/pdb7zw6/pdb
• EMDBエントリー: 14993
• 分子名称: Slr0869 protein (1 entity in total)
• 機能のキーワード: bdlp, cyanobacteria, membrane remodeling, lipid binding protein
• 由来する生物種: Synechocystis sp. PCC 6803
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 749643.18

構造登録者

Gewehr, L.,Junglas, B.,Jilly, R.,Franz, J.,Wenyu, E.Z.,Weidner, T.,Bonn, M.,Sachse, C.,Schneider, D. (登録日: 2022-05-18, 公開日: 2023-04-19, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.7 Å)