7AL2

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

Summary for 7AL2

• Entry DOI: 10.2210/pdb7al2/pdb
• Related: 7AL1
• Descriptor: Cell division protein SepF, Cell division protein FtsZ (2 entities in total)
• Functional Keywords: ftsz-binding protein membrane-binding protein, cell cycle
• Biological source: Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS); More
• Total number of polymer chains: 2
• Total formula weight: 12033.76

Authors

Sogues, A.,Wehenkel, A.M.,Alzari, P.M. (deposition date: 2020-10-04, release date: 2021-03-31, Last modification date: 2024-01-31)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.701 Å)