2c9b

From Proteopedia

Revision as of 14:57, 30 October 2007

LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-TRIHYDRO-9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL)

Overview

Recently published genomic investigations of the human pathogen, Mycobacterium tuberculosis have revealed that genes coding the proteins, involved in riboflavin biosynthesis are essential for the growth of the, organism. Because the enzymes involved in cofactor biosynthesis pathways, are not present in humans, they appear to be promising candidates for the, development of therapeutic drugs. The substituted purinetrione compounds, have demonstrated high affinity and specificity to lumazine synthase, which catalyzes the penultimate step of riboflavin biosynthesis in, bacteria and plants. The structure of M. tuberculosis lumazine synthase in, complex with five different inhibitor compounds is presented, together, with studies of the binding reactions by isothermal titration calorimetry., The ... [(full description)]

About this Structure

2C9B is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with K, PO4, PUG and MPD as [ligands]. Active as [Riboflavin synthase], with EC number [2.5.1.9]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural and thermodynamic insights into the binding mode of five novel inhibitors of lumazine synthase from Mycobacterium tuberculosis., Morgunova E, Illarionov B, Sambaiah T, Haase I, Bacher A, Cushman M, Fischer M, Ladenstein R, FEBS J. 2006 Oct;273(20):4790-804. Epub 2006 Sep 19. PMID:16984393

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