5OXF

An oligomerised bacterial dynamin pair provides a mechanism for the long range sensing and tethering of membranes

5OXF の概要

• エントリーDOI: 10.2210/pdb5oxf/pdb
• 関連するPDBエントリー: 5OWV
• 分子名称: GTP-binding protein, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: dynamin, membrane remodelling, membrane fusion, membrane tethering., lipid binding protein
• 由来する生物種: Campylobacter jejuni; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 316109.10

構造登録者

Liu, J.W.,Noel, J.K.,Low, H.H. (登録日: 2017-09-06, 公開日: 2018-09-05, 最終更新日: 2024-05-08)

主引用文献

Liu, J.,Noel, J.K.,Low, H.H.
Structural basis for membrane tethering by a bacterial dynamin-like pair.
Nat Commun, 9:3345-3345, 2018

PubMed Abstract: Dynamin-like proteins (DLPs) are large GTPases that restructure membrane. DLPs such as the mitofusins form heterotypic oligomers between isoform pairs that bridge and fuse opposing membranes. In bacteria, heterotypic oligomerisation may also be important for membrane remodelling as most DLP genes are paired within operons. How DLPs tether opposing membranes is unknown. Here we show the crystal structure of a DLP heterotypic pair from the pathogen Campylobacter jejuni. A 2:2 stoichiometric tetramer is observed where heterodimers, conjoined by a random coil linker, assemble back-to-back to form a tripartite DLP chain with extreme flexibility. In vitro, tetramerisation triggers GTPase activity and induces lipid binding. Liposomes are readily tethered and form tubes at high tetramer concentration. Our results provide a direct mechanism for the long-range binding and bridging of opposing membranes by a bacterial DLP pair. They also provide broad mechanistic and structural insights that are relevant to other heterotypic DLP complexes.

PubMed: 30131557
DOI: 10.1038/s41467-018-05523-8

実験手法

X-RAY DIFFRACTION (3.94 Å)