5H5G

Staphylococcus aureus FtsZ-GDP in T and R states

5H5G の概要

• エントリーDOI: 10.2210/pdb5h5g/pdb
• 関連するPDBエントリー: 5H5H 5H5I
• 分子名称: Cell division protein FtsZ, GUANOSINE-5'-DIPHOSPHATE, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: tubulin/ftsz family, gtpase, protofilament, cell cycle
• 由来する生物種: Staphylococcus aureus (strain MRSA252)
• 細胞内の位置: Cytoplasm : Q6GHP9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64632.53

構造登録者

Fujita, J.,Harada, R.,Maeda, Y.,Saito, Y.,Mizohata, E.,Inoue, T.,Shigeta, Y.,Matsumura, H. (登録日: 2016-11-05, 公開日: 2017-05-24, 最終更新日: 2023-11-08)

主引用文献

Fujita, J.,Harada, R.,Maeda, Y.,Saito, Y.,Mizohata, E.,Inoue, T.,Shigeta, Y.,Matsumura, H.
Identification of the key interactions in structural transition pathway of FtsZ from Staphylococcus aureus
J. Struct. Biol., 198:65-73, 2017

PubMed Abstract: The tubulin-homolog protein FtsZ is essential for bacterial cell division. FtsZ polymerizes to form protofilaments that assemble into a contractile ring-shaped structure in the presence of GTP. Recent studies showed that FtsZ treadmilling coupled with the GTPase activity drives cell wall synthesis and bacterial cell division. The treadmilling caused by assembly and disassembly of FtsZ links to a conformational change of the monomer from a tense (T) to a relaxed (R) state, but considerable controversy still remains concerning the mechanism. In this study, we report crystal structures of FtsZ from Staphylococcus aureus corresponding to the T and R state conformations in the same crystal, indicating the structural equilibrium of the two state. The two structures identified a key residue Arg29, whose importance was also confirmed by our modified MD simulations. Crystal structures of the R29A mutant showed T and R state-like conformations with slight but important structural changes compared to those of wild-type. Collectively, these data provide new insights for understanding how intramolecular interactions are related to the structural transition of FtsZ.

PubMed: 28456664
DOI: 10.1016/j.jsb.2017.04.008

実験手法

X-RAY DIFFRACTION (2.2 Å)