4V7G

Crystal Structure of Lumazine Synthase from Bacillus Anthracis

これはPDB形式変換不可エントリーです。

4V7G の概要

• エントリーDOI: 10.2210/pdb4v7g/pdb
• 分子名称: 6,7-dimethyl-8-ribityllumazine synthase, PHOSPHATE ION (2 entities in total)
• 機能のキーワード: transferase, riboflavin biosynthesis
• 由来する生物種: Bacillus Anthracis
• タンパク質・核酸の鎖数: 90
• 化学式量合計: 1473176.43

構造登録者

Morgunova, E.,Illarionov, B.,Saller, S.,Popov, A.,Sambaiah, T.,Bacher, A.,Cushman, M.,Fischer, M.,Ladenstein, R. (登録日: 2009-09-16, 公開日: 2014-07-09, 最終更新日: 2023-09-20)

主引用文献

Morgunova, E.,Illarionov, B.,Saller, S.,Popov, A.,Sambaiah, T.,Bacher, A.,Cushman, M.,Fischer, M.,Ladenstein, R.
Structural study and thermodynamic characterization of inhibitor binding to lumazine synthase from Bacillus anthracis.
Acta Crystallogr.,Sect.D, 66:1001-1011, 2010

PubMed Abstract: The crystal structure of lumazine synthase from Bacillus anthracis was solved by molecular replacement and refined to R(cryst) = 23.7% (R(free) = 28.4%) at a resolution of 3.5 A. The structure reveals the icosahedral symmetry of the enzyme and specific features of the active site that are unique in comparison with previously determined orthologues. The application of isothermal titration calorimetry in combination with enzyme kinetics showed that three designed pyrimidine derivatives bind to lumazine synthase with micromolar dissociation constants and competitively inhibit the catalytic reaction. Structure-based modelling suggested the binding modes of the inhibitors in the active site and allowed an estimation of the possible contacts formed upon binding. The results provide a structural framework for the design of antibiotics active against B. anthracis.

PubMed: 20823551
DOI: 10.1107/S0907444910029690

実験手法

X-RAY DIFFRACTION (3.5 Å)