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-Structure paper
タイトル | SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 2156, Year 2023 |
掲載日 | 2023年4月14日 |
著者 | Lucas Gewehr / Benedikt Junglas / Ruven Jilly / Johannes Franz / Wenyu Eva Zhu / Tobias Weidner / Mischa Bonn / Carsten Sachse / Dirk Schneider / |
PubMed 要旨 | 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- ...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. |
リンク | Nat Commun / PubMed:37059718 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.7 Å |
構造データ | EMDB-14993, PDB-7zw6: |
由来 |
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キーワード | LIPID BINDING PROTEIN / BDLP / cyanobacteria (藍藻) / membrane remodeling |