4V7G

Crystal Structure of Lumazine Synthase from Bacillus Anthracis

This is a non-PDB format compatible entry.

Summary for 4V7G

• Entry DOI: 10.2210/pdb4v7g/pdb
• Descriptor: 6,7-dimethyl-8-ribityllumazine synthase, PHOSPHATE ION (2 entities in total)
• Functional Keywords: transferase, riboflavin biosynthesis
• Biological source: Bacillus Anthracis
• Total number of polymer chains: 90
• Total formula weight: 1473176.43

Authors

Morgunova, E.,Illarionov, B.,Saller, S.,Popov, A.,Sambaiah, T.,Bacher, A.,Cushman, M.,Fischer, M.,Ladenstein, R. (deposition date: 2009-09-16, release date: 2014-07-09, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.5 Å)