1W5F

FtsZ, T7 mutated, domain swapped (T. maritima)

Summary for 1W5F

• Entry DOI: 10.2210/pdb1w5f/pdb
• Related: 1FSZ 1W58 1W59 1W5A 1W5B 1W5E
• Descriptor: CELL DIVISION PROTEIN FTSZ, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: cell division, cell-division protein, gtp-binding, multigene family, septation, tubulin, ftsz, filament, z-ring, gtpase, domain swapped
• Biological source: THERMOTOGA MARITIMA
• Cellular location: Cytoplasm : O08398
• Total number of polymer chains: 2
• Total formula weight: 78437.88

Authors

Oliva, M.A.,Cordell, S.C.,Lowe, J. (deposition date: 2004-08-06, release date: 2004-12-01, Last modification date: 2023-12-13)

Primary citation

Oliva, M.A.,Cordell, S.C.,Lowe, J.
Structural Insights Into Ftsz Protofilament Formation
Nat.Struct.Mol.Biol., 11:1243-, 2004

PubMed Abstract: The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure essential for bacterial cell division. We have used refolded FtsZ to crystallize a tubulin-like protofilament. The N- and C-terminal domains of two consecutive subunits in the filament assemble to form the GTPase site, with the C-terminal domain providing water-polarizing residues. A domain-swapped structure of FtsZ and biochemical data on purified N- and C-terminal domains show that they are independent. This leads to a model of how FtsZ and tubulin polymerization evolved by fusing two domains. In polymerized tubulin, the nucleotide-binding pocket is occluded, which leads to nucleotide exchange being the rate-limiting step and to dynamic instability. In our FtsZ filament structure the nucleotide is exchangeable, explaining why, in this filament, nucleotide hydrolysis is the rate-limiting step during FtsZ polymerization. Furthermore, crystal structures of FtsZ in different nucleotide states reveal notably few differences.

PubMed: 15558053
DOI: 10.1038/NSMB855

Experimental method

X-RAY DIFFRACTION (2 Å)