9V7V

Structure of FtsZ1 in complex with GMPCPP from Candidatus Odinarchaeota

Summary for 9V7V

• Entry DOI: 10.2210/pdb9v7v/pdb
• EMDB information: 64825
• Descriptor: Cell division protein FtsZ, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER (2 entities in total)
• Functional Keywords: cell division protein, cell cycle
• Biological source: Candidatus Odinarchaeota
• Total number of polymer chains: 4
• Total formula weight: 157055.94

Authors

Bose, S.,Kutti, R.V. (deposition date: 2025-05-28, release date: 2025-07-30, Last modification date: 2025-11-19)

Primary citation

Kumari, J.,Uthaman, A.,Bose, S.,Kundu, A.,Sharma, V.,Dutta, S.,Dhar, A.,Roy, S.,Srinivasan, R.,Pande, S.,Vinothkumar, K.R.,Gayathri, P.,Palani, S.
Distinct filament morphology and membrane tethering features of the dual FtsZ paralogs in Odinarchaeota.
Embo J., 44:5940-5964, 2025

PubMed Abstract: The Asgard phylum has emerged as a model to study eukaryogenesis because of their close relatedness with the eukaryotes. In this study, we use FtsZ proteins from a member of the class Odinarchaeia as representatives to investigate the probable origin, evolution, and assembly of the FtsZ/tubulin protein superfamily in Asgard archaea. We performed a comparative analysis of the biochemical properties and cytoskeletal assembly of FtsZ1 and FtsZ2, the two FtsZ isoforms in the Odinarchaeota metagenome. Our electron microscopy analysis reveals that OdinFtsZ1 assembles into curved single protofilaments, while OdinFtsZ2 forms stacked spiral ring-like structures. Upon sequence analysis, we identified an N-terminal amphipathic helix in OdinFtsZ1, which mediates direct membrane tethering. In contrast, OdinFtsZ2 is recruited to the membrane by the anchor OdinSepF via OdinFtsZ2's C-terminal tail. Overall, we report the presence of two distant evolutionary paralogs of FtsZ in Odinarchaeota, with distinct filament assemblies and differing modes of membrane targeting. Our findings highlight the diversity of FtsZ proteins in the archaeal phylum Asgardarchaeota, providing valuable insights into the evolution and differentiation of tubulin-family proteins.

PubMed: 40781499
DOI: 10.1038/s44318-025-00529-7

Experimental method

ELECTRON MICROSCOPY (3.6 Å)