1di0

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1di0, resolution 2.7Å

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CRYSTAL STRUCTURE OF LUMAZINE SYNTHASE FROM BRUCELLA ABORTUS

Overview

We have determined the three-dimensional structure of 6, 7-dimethyl-8-ribityllumazine synthase (lumazine synthase) from Brucella, abortus, the infectious organism of the disease brucellosis in animals., This enzyme catalyses the formation of 6, 7-dimethyl-8-ribityllumazine, the penultimate product in the synthesis of riboflavin. The, three-dimensional X-ray crystal structure of the enzyme from B. abortus, has been solved and refined at 2.7 A resolution to a final R-value of 0.18, (R(free)=0.23). The macromolecular assembly of the enzyme differs from, that of the enzyme from Bacillus subtilis, the only other lumazine, synthase structure known. While the protein from B. subtilis assembles, into a 60 subunit icosahedral capsid built from 12 pentameric units, the, enzyme from B. abortus is pentameric in its crystalline form. Nonetheless, the active sites of the two enzymes are virtually identical indicating, inhibitors to theses enzymes could be effective pharmaceuticals across a, broad species range. Furthermore, we compare the structures of the enzyme, from B. subtilis and B. abortus and describe the C teminus structure which, accounts for the differences in quaternary structure.

About this Structure

1DI0 is a Single protein structure of sequence from Brucella abortus with PO4 as ligand. Full crystallographic information is available from OCA.

Reference

Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus., Braden BC, Velikovsky CA, Cauerhff AA, Polikarpov I, Goldbaum FA, J Mol Biol. 2000 Apr 14;297(5):1031-6. PMID:10764570

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