6GAU

Extremely 'open' clamp structure of DNA gyrase: role of the Corynebacteriales GyrB specific insert

6GAU の概要

• エントリーDOI: 10.2210/pdb6gau/pdb
• 分子名称: DNA gyrase subunit B,DNA gyrase subunit A, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: mycobacterium tuberculosis topoisomerase dna gyrase, dna binding protein
• 由来する生物種: Mycobacterium tuberculosis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 261959.72

構造登録者

Petrella, S.,Capton, E.,Alzari, P.M.,Aubry, A.,Mayer, C. (登録日: 2018-04-12, 公開日: 2019-02-20, 最終更新日: 2024-01-17)

主引用文献

Petrella, S.,Capton, E.,Raynal, B.,Giffard, C.,Thureau, A.,Bonnete, F.,Alzari, P.M.,Aubry, A.,Mayer, C.
Overall Structures of Mycobacterium tuberculosis DNA Gyrase Reveal the Role of a Corynebacteriales GyrB-Specific Insert in ATPase Activity.
Structure, 27:579-589.e5, 2019

PubMed Abstract: Despite sharing common features, previous studies have shown that gyrases from different species have been modified throughout evolution to modulate their properties. Here, we report two crystal structures of Mycobacterium tuberculosis DNA gyrase, an apo and AMPPNP-bound form at 2.6-Å and 3.3-Å resolution, respectively. These structures provide high-resolution structural data on the quaternary organization and interdomain connections of a gyrase (full-length GyrB-GyrA57) thus providing crucial inputs on this essential drug target. Together with small-angle X-ray scattering studies, they revealed an "extremely open" N-gate state, which persists even in the DNA-free gyrase-AMPPNP complex and an unexpected connection between the ATPase and cleavage core domains mediated by two Corynebacteriales-specific motifs, respectively the C-loop and DEEE-loop. We show that the C-loop participates in the stabilization of this open conformation, explaining why this gyrase has a lower ATPase activity. Our results image a conformational state which might be targeted for drug discovery.

PubMed: 30744994
DOI: 10.1016/j.str.2019.01.004

実験手法

X-RAY DIFFRACTION (3.3 Å)