1RQ2

MYCOBACTERIUM TUBERCULOSIS FTSZ IN COMPLEX WITH CITRATE

1RQ2 の概要

• エントリーDOI: 10.2210/pdb1rq2/pdb
• 関連するPDBエントリー: 1RLU 1RQ7
• 分子名称: Cell division protein ftsZ, CITRIC ACID (3 entities in total)
• 機能のキーワード: cell cycle, tubulin, gtpase, signaling protein
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78338.13

構造登録者

Leung, A.K.W.,White, E.L.,Ross, L.J.,Reynolds, R.C.,DeVito, J.A.,Borhani, D.W. (登録日: 2003-12-04, 公開日: 2004-08-31, 最終更新日: 2023-08-23)

主引用文献

Leung, A.K.,Lucile White, E.,Ross, L.J.,Reynolds, R.C.,DeVito, J.A.,Borhani, D.W.
Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches.
J.Mol.Biol., 342:953-970, 2004

PubMed Abstract: We report three crystal structures of the Mycobacterium tuberculosis cell division protein FtsZ, as the citrate, GDP, and GTPgammaS complexes, determined at 1.89, 2.60, and 2.08A resolution. MtbFtsZ crystallized as a tight, laterally oriented dimer distinct from the longitudinal polymer observed for alphabeta-tubulin. Mutational data on Escherichia coli FtsZ suggest that this dimer interface is important for proper protofilament and "Z-ring" assembly and function. An alpha-to-beta secondary structure conformational switch at the dimer interface is spatially analogous to, and has many of the hallmarks of, the Switch I conformational changes exhibited by G-proteins upon activation. The presence of a gamma-phosphate in the FtsZ active site modulates the conformation of the "tubulin" loop T3 (spatially analogous to the G-protein Switch II); T3 switching upon gamma-phosphate ligation is directly coupled to the alpha-to-beta switch by steric overlap. The dual conformational switches observed here for the first time in an FtsZ link GTP binding and hydrolysis to FtsZ (and tubulin) lateral assembly and Z-ring contraction, and they are suggestive of an underappreciated functional analogy between FtsZ, tubulin and G-proteins.

PubMed: 15342249
DOI: 10.1016/j.jmb.2004.07.061

実験手法

X-RAY DIFFRACTION (1.86 Å)