2a57
From Proteopedia
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Structure of 6,7-Dimthyl-8-ribityllumazine synthase from Schizosaccharomyces pombe mutant W27Y with bound ligand 6-carboxyethyl-7-oxo-8-ribityllumazine
Overview
The amino acid residue tryptophan 27 of 6,7-dimethyl-8-ribityllumazine, synthase of the yeast Schizosaccharomyces pombe was replaced by tyrosine., The structures of the W27Y mutant protein in complex with riboflavin, the, substrate analogue 5-nitroso-6-ribitylamino-2,4(1H,3H)-pyrimidinedione, and the product analogue 6-carboxyethyl-7-oxo-8-ribityllumazine, were, determined by X-ray crystallography at resolutions of 2.7-2.8 A. Whereas, the indole system of W27 forms a coplanar pi-complex with riboflavin, the, corresponding phenyl ring in the W27Y mutant establishes only peripheral, contact with the heterocyclic ring system of the bound riboflavin. These, findings provide an explanation for the absence of the long wavelength, shift in optical absorption spectra of riboflavin bound to the mutant, enzyme. The structures of the mutants are important tools for the, interpretation of the unusual physical properties of riboflavin in complex, with lumazine synthase.
About this Structure
2A57 is a Single protein structure of sequence from Schizosaccharomyces pombe with PO4 and CRM as ligands. Active as Riboflavin synthase, with EC number 2.5.1.9 Full crystallographic information is available from OCA.
Reference
Structural basis of charge transfer complex formation by riboflavin bound to 6,7-dimethyl-8-ribityllumazine synthase., Koch M, Breithaupt C, GerhardtHaase S, Weber S, Cushman M, Huber R, Bacher A, Fischer M, Eur J Biochem. 2004 Aug;271(15):3208-14. PMID:15265040
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