1TKU

Crystal Structure of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans in complex with Ribulose-5-phosphate

Summary for 1TKU

• Entry DOI: 10.2210/pdb1tku/pdb
• Descriptor: 3,4-Dihydroxy-2-butanone 4-phosphate Synthase, RIBULOSE-5-PHOSPHATE (3 entities in total)
• Functional Keywords: candida albicans, riboflavin biosynthesis, 3, 4-dihydroxy-2-butanone 4-phosphate synthase, synthetic gene, isomerase
• Biological source: Candida albicans
• Total number of polymer chains: 2
• Total formula weight: 45830.18

Authors

Echt, S.,Bauer, S.,Steinbacher, S.,Huber, R.,Bacher, A.,Fischer, M. (deposition date: 2004-06-09, release date: 2004-09-07, Last modification date: 2023-08-23)

Primary citation

Echt, S.,Bauer, S.,Steinbacher, S.,Huber, R.,Bacher, A.,Fischer, M.
Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans.
J.Mol.Biol., 341:1085-1096, 2004

PubMed 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 angstroms, 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.

PubMed: 15328619
DOI: 10.1016/j.jmb.2004.06.053

Experimental method

X-RAY DIFFRACTION (1.66 Å)