1W58

FtsZ GMPCPP soak I213 (M. jannaschii)

1W58 の概要

• エントリーDOI: 10.2210/pdb1w58/pdb
• 関連するPDBエントリー: 1FSZ 1W59 1W5A 1W5B 1W5E
• 分子名称: CELL DIVISION PROTEIN FTSZ HOMOLOG 1, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: cell division, cell division protein, cell-division protein, ftsz, gtp-binding, multigene family, septation, tubulin
• 由来する生物種: METHANOCALDOCOCCUS JANNASCHII
• 細胞内の位置: Cytoplasm : Q57816
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39515.64

構造登録者

Oliva, M.A.,Cordell, S.C.,Lowe, J. (登録日: 2004-08-06, 公開日: 2004-12-01, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)