2ZJT

Crystal structure of dna gyrase B' domain sheds lights on the mechanism for T-segment navigation

2ZJT の概要

• エントリーDOI: 10.2210/pdb2zjt/pdb
• 関連するPDBエントリー: 1AB4 1BGW 1BJT 1EI1 1SUU 2NOV 2RGR
• 分子名称: DNA gyrase subunit B (1 entity in total)
• 機能のキーワード: dna gyrase, gyrb-ctd, toprim, tail, dna topoisomerase ii, g-segment, t-segment, atp-binding, nucleotide-binding, isomerase
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cytoplasm (Potential): P0C5C5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55874.02

構造登録者

Fu, G.S.,Zhu, D.Y.,Hu, Y.L.,Wang, D.C. (登録日: 2008-03-10, 公開日: 2009-03-10, 最終更新日: 2024-03-13)

主引用文献

Fu, G.S.,Wu, J.J.,Liu, W.,Zhu, D.Y.,Hu, Y.L.,Deng, J.,Zhang, X.E.,Bi, L.J.,Wang, D.C.
Crystal structure of DNA gyrase B' domain sheds lights on the mechanism for T-segment navigation
Nucleic Acids Res., 37:5908-5916, 2009

PubMed Abstract: DNA gyrase is an indispensible marvelous molecular machine in manipulating the DNA topology for the prokaryotes. In the 'two-gate' mechanism of DNA topoisomerase, T-segment navigation from N- to DNA-gate is a critical step, but the structural basis supporting this scheme is unclear. The crystal structure of DNA gyrase B' subfragment from Mycobacterium tuberculosis reveals an intrinsic homodimer. The two subunits, each consisting of a Tail and a Toprim domain, are tightly packed one another to form a 'crab-like' organization never observed previously from yeast topo II. Structural comparisons show two orientational alterations of the Tail domain, which may be dominated by a 43-residue peptide at the B' module C-terminus. A highly conserved pentapeptide mediates large-scale intrasubunit conformational change as a hinge point. Mutational studies highlight the significant roles of a negatively charge cluster on a groove at dimer interface. On the basis of structural analysis and mutation experiments, a sluice-like model for T-segment transport is proposed.

PubMed: 19596812
DOI: 10.1093/nar/gkp586

実験手法

X-RAY DIFFRACTION (2.8 Å)