2riu: Difference between revisions

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.

2RIU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans] with <scene name='pdbligand=5RP:'>5RP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:5rp Binding Site For Residue A 701'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIU OCA].  

Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans., Echt S, Bauer S, Steinbacher S, Huber R, Bacher A, Fischer M, J Mol Biol. 2004 Aug 20;341(4):1085-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15328619 15328619]

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