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spinqualitylabelsall models 1kzl, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Riboflavin Synthase from S.pombe bound to Carboxyethyllumazine

Overview

Riboflavin synthase catalyzes the disproportionation of, 6,7-dimethyl-8-ribityllumazine affording riboflavin and, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. We have determined the, structure of riboflavin synthase from Schizosaccharomyces pombe in complex, with the substrate analog, 6-carboxyethyl-7-oxo-8-ribityllumazine at 2.1 A, resolution. In contrast to the homotrimeric solution state of native, riboflavin synthase, we found the enzyme to be monomeric in the crystal, structure. Structural comparison of the riboflavin synthases of S. pombe, and Escherichia coli suggests oligomer contact sites and delineates the, catalytic site for dimerization of the substrate and subsequent, fragmentation of the pentacyclic intermediate. The pentacyclic substrate, dimer was modeled into the proposed active site, and its stereochemical, features were determined. The model suggests that the substrate molecule, at the C-terminal domain donates a four-carbon unit to the substrate, molecule bound at the N-terminal domain of an adjacent subunit in the, oligomer.

About this Structure

1KZL is a Single protein structure of sequence from Schizosaccharomyces pombe with HG and CRM as ligands. Active as Riboflavin synthase, with EC number 2.5.1.9 Full crystallographic information is available from OCA.

Reference

Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine., Gerhardt S, Schott AK, Kairies N, Cushman M, Illarionov B, Eisenreich W, Bacher A, Huber R, Steinbacher S, Fischer M, Structure. 2002 Oct;10(10):1371-81. PMID:12377123

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