1iez

From Proteopedia

Revision as of 15:13, 20 November 2007

Solution Structure of 3,4-Dihydroxy-2-Butanone 4-Phosphate Synthase of Riboflavin Biosynthesis

Overview

Recent developments in NMR have extended the size range of proteins, amenable to structural and functional characterization to include many, larger proteins involved in important cellular processes. By applying a, combination of residue-specific isotope labeling and protein deuteration, strategies tailored to yield specific information, we were able to, determine the solution structure and study structure-activity, relationships of 3,4-dihydroxy-2-butanone-4-phosphate synthase, a 47-kDa, enzyme from the Escherichia coli riboflavin biosynthesis pathway and an, attractive target for novel antibiotics. Our investigations of the, enzyme's ligand binding by NMR and site-directed mutagenesis yields a, conclusive picture of the location and identity of residues directly, involved in substrate binding and catalysis. Our studies illustrate the, power of state-of-the-art NMR techniques for the structural, characterization and investigation of ligand binding in protein complexes, approaching the 50-kDa range in solution.

About this Structure

1IEZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site., Kelly MJ, Ball LJ, Krieger C, Yu Y, Fischer M, Schiffmann S, Schmieder P, Kuhne R, Bermel W, Bacher A, Richter G, Oschkinat H, Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13025-30. Epub 2001 Oct 30. PMID:11687623

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