4A2B
Thermotoga maritima FtsA with ATP gamma S
Summary for 4A2B
Entry DOI | 10.2210/pdb4a2b/pdb |
Related | 1E4F 1E4G 4A2A |
Descriptor | CELL DIVISION PROTEIN FTSA, PUTATIVE, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | cell cycle, actin-like, filament |
Biological source | THERMOTOGA MARITIMA |
Total number of polymer chains | 1 |
Total formula weight | 47623.29 |
Authors | Szwedziak, P.,Lowe, J. (deposition date: 2011-09-23, release date: 2012-04-25, Last modification date: 2023-12-20) |
Primary citation | Szwedziak, P.,Wang, Q.,Freund, S.M.V.,Lowe, J. Ftsa Forms Actin-Like Protofilaments Embo J., 31:2249-, 2012 Cited by PubMed Abstract: FtsA is an early component of the Z-ring, the structure that divides most bacteria, formed by tubulin-like FtsZ. FtsA belongs to the actin family of proteins, showing an unusual subdomain architecture. Here we reconstitute the tethering of FtsZ to the membrane via FtsA's C-terminal amphipathic helix in vitro using Thermotoga maritima proteins. A crystal structure of the FtsA:FtsZ interaction reveals 16 amino acids of the FtsZ tail bound to subdomain 2B of FtsA. The same structure and a second crystal form of FtsA reveal that FtsA forms actin-like protofilaments with a repeat of 48 Å. The identical repeat is observed when FtsA is polymerized using a lipid monolayer surface and FtsAs from three organisms form polymers in cells when overexpressed, as observed by electron cryotomography. Mutants that disrupt polymerization also show an elongated cell division phenotype in a temperature-sensitive FtsA background, demonstrating the importance of filament formation for FtsA's function in the Z-ring. PubMed: 22473211DOI: 10.1038/EMBOJ.2012.76 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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