6SAT

Cell Division Protein SepF in complex with C-terminal domain of FtsZ

Summary for 6SAT

• Entry DOI: 10.2210/pdb6sat/pdb
• Descriptor: Cell division protein SepF, Cell division protein FtsZ (3 entities in total)
• Functional Keywords: cell division protein, cell cycle
• Biological source: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025); More
• Total number of polymer chains: 4
• Total formula weight: 22193.11

Authors

Sogues, A.,Wehenkel, A.M.,Alzari, P.M. (deposition date: 2019-07-17, release date: 2020-03-11, Last modification date: 2024-05-15)

Primary citation

Sogues, A.,Martinez, M.,Gaday, Q.,Ben Assaya, M.,Grana, M.,Voegele, A.,VanNieuwenhze, M.,England, P.,Haouz, A.,Chenal, A.,Trepout, S.,Duran, R.,Wehenkel, A.M.,Alzari, P.M.
Essential dynamic interdependence of FtsZ and SepF for Z-ring and septum formation in Corynebacterium glutamicum.
Nat Commun, 11:1641-1641, 2020

PubMed Abstract: The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane anchors and Z-ring regulators described for E. coli. Here we investigate the physiological function of Corynebacterium glutamicum SepF, the only cell division-associated protein from Actinobacteria known to interact with the conserved C-terminal tail of FtsZ. We show an essential interdependence of FtsZ and SepF for formation of a functional Z-ring in C. glutamicum. The crystal structure of the SepF-FtsZ complex reveals a hydrophobic FtsZ-binding pocket, which defines the SepF homodimer as the functional unit, and suggests a reversible oligomerization interface. FtsZ filaments and lipid membranes have opposing effects on SepF polymerization, indicating that SepF has multiple roles at the cell division site, involving FtsZ bundling, Z-ring tethering and membrane reshaping activities that are needed for proper Z-ring assembly and function.

PubMed: 32242019
DOI: 10.1038/s41467-020-15490-8

Experimental method

X-RAY DIFFRACTION (1.6 Å)