Potential Anti-infective Targets in Pathogenic Yeasts: Structure and Properties of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans

Echt, Stefanie, Bauer, Stefanie, Steinbacher, Stefan, Huber, Robert, Bacher, Adelbert and Fischer, Markus 2004. Potential Anti-infective Targets in Pathogenic Yeasts: Structure and Properties of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans. Journal of Molecular Biology 341 (4) , pp. 1085-1096. 10.1016/j.jmb.2004.06.053

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Abstract

A synthetic gene specifying a putative 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans directed the synthesis of a 22.5 kDa peptide in a recombinant Escherichia coli strain. The recombinant protein was purified to apparent homogeneity by two chromatographic steps and was shown to catalyze the formation of l-3,4-dihydroxy-2-butanone 4-phosphate from ribulose 5-phosphate at a rate of 332 nmol mg−1 min−1. Hydrodynamic studies indicated a native molecular mass of 41 kDa in line with a homodimer structure. The protein was crystallized in its apoform. Soaking yielded crystals in complex with the substrate ribulose 5-phosphate. The structures were solved at resolutions of 1.6 and 1.7 Å, respectively, using 3,4-dihydroxy-2-butanone 4-phosphate synthase of E. coli for molecular replacement. Structural comparison with the orthologs of Magnaporthe grisea and Methanococcus jannaschii revealed a hitherto unknown conformation of the essential acidic active-site loop.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Publisher:	Elsevier
ISSN:	0022-2836
Last Modified:	24 Jun 2017 11:00
URI:	https://orca.cardiff.ac.uk/id/eprint/70157

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