7AL2

Cell division protein SepF from Methanobrevibacter smithii in complex with FtsZ-CTD

7AL2 の概要

• エントリーDOI: 10.2210/pdb7al2/pdb
• 関連するPDBエントリー: 7AL1
• 分子名称: Cell division protein SepF, Cell division protein FtsZ (2 entities in total)
• 機能のキーワード: ftsz-binding protein membrane-binding protein, cell cycle
• 由来する生物種: Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12033.76

構造登録者

Sogues, A.,Wehenkel, A.M.,Alzari, P.M. (登録日: 2020-10-04, 公開日: 2021-03-31, 最終更新日: 2024-01-31)

主引用文献

Pende, N.,Sogues, A.,Megrian, D.,Sartori-Rupp, A.,England, P.,Palabikyan, H.,Rittmann, S.K.R.,Grana, M.,Wehenkel, A.M.,Alzari, P.M.,Gribaldo, S.
SepF is the FtsZ anchor in archaea, with features of an ancestral cell division system.
Nat Commun, 12:3214-3214, 2021

PubMed Abstract: Most archaea divide by binary fission using an FtsZ-based system similar to that of bacteria, but they lack many of the divisome components described in model bacterial organisms. Notably, among the multiple factors that tether FtsZ to the membrane during bacterial cell constriction, archaea only possess SepF-like homologs. Here, we combine structural, cellular, and evolutionary analyses to demonstrate that SepF is the FtsZ anchor in the human-associated archaeon Methanobrevibacter smithii. 3D super-resolution microscopy and quantitative analysis of immunolabeled cells show that SepF transiently co-localizes with FtsZ at the septum and possibly primes the future division plane. M. smithii SepF binds to membranes and to FtsZ, inducing filament bundling. High-resolution crystal structures of archaeal SepF alone and in complex with the FtsZ C-terminal domain (FtsZ) reveal that SepF forms a dimer with a homodimerization interface driving a binding mode that is different from that previously reported in bacteria. Phylogenetic analyses of SepF and FtsZ from bacteria and archaea indicate that the two proteins may date back to the Last Universal Common Ancestor (LUCA), and we speculate that the archaeal mode of SepF/FtsZ interaction might reflect an ancestral feature. Our results provide insights into the mechanisms of archaeal cell division and pave the way for a better understanding of the processes underlying the divide between the two prokaryotic domains.

PubMed: 34088904
DOI: 10.1038/s41467-021-23099-8

実験手法

X-RAY DIFFRACTION (2.701 Å)