7Q6F

Vibrio maritimus FtsA 1-396 ATP, double filament

Summary for 7Q6F

• Entry DOI: 10.2210/pdb7q6f/pdb
• Descriptor: Cell division protein FtsA, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• Functional Keywords: bacterial cell division, divisome, actin homologue, cell cycle
• Biological source: Vibrio maritimus
• Total number of polymer chains: 2
• Total formula weight: 86126.59

Authors

Nierhaus, T.,Kureisaite-Ciziene, D.,Lowe, J. (deposition date: 2021-11-07, release date: 2022-09-21, Last modification date: 2024-01-31)

Primary citation

Nierhaus, T.,McLaughlin, S.H.,Burmann, F.,Kureisaite-Ciziene, D.,Maslen, S.L.,Skehel, J.M.,Yu, C.W.H.,Freund, S.M.V.,Funke, L.F.H.,Chin, J.W.,Lowe, J.
Bacterial divisome protein FtsA forms curved antiparallel double filaments when binding to FtsN.
Nat Microbiol, 7:1686-1701, 2022

PubMed Abstract: During bacterial cell division, filaments of tubulin-like FtsZ form the Z-ring, which is the cytoplasmic scaffold for divisome assembly. In Escherichia coli, the actin homologue FtsA anchors the Z-ring to the membrane and recruits divisome components, including bitopic FtsN. FtsN regulates the periplasmic peptidoglycan synthase FtsWI. To characterize how FtsA regulates FtsN, we applied electron microscopy to show that E. coli FtsA forms antiparallel double filaments on lipid monolayers when bound to the cytoplasmic tail of FtsN. Using X-ray crystallography, we demonstrate that Vibrio maritimus FtsA crystallizes as an equivalent double filament. We identified an FtsA-FtsN interaction site in the IA-IC interdomain cleft of FtsA using X-ray crystallography and confirmed that FtsA forms double filaments in vivo by site-specific cysteine cross-linking. FtsA-FtsN double filaments reconstituted in or on liposomes prefer negative Gaussian curvature, like those of MreB, the actin-like protein of the elongasome. We propose that curved antiparallel FtsA double filaments together with treadmilling FtsZ filaments organize septal peptidoglycan synthesis in the division plane.

PubMed: 36123441
DOI: 10.1038/s41564-022-01206-9

Experimental method

X-RAY DIFFRACTION (3.31 Å)