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1TKS

Crystal structure of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans

Summary for 1TKS
Entry DOI10.2210/pdb1tks/pdb
Related1TKU
Descriptor3,4-dihydroxy-2-butanone 4-phosphate synthase (2 entities in total)
Functional Keywordscandida albicans, riboflavin biosynthesis, 3, 4-dihydroxy-2-butanone 4-phosphate synthase, crystal structure synthetic gene, isomerase
Biological sourceCandida albicans
Total number of polymer chains2
Total formula weight45369.96
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 citationEcht, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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