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2riu

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(New page: 200px<br /><applet load="2riu" size="350" color="white" frame="true" align="right" spinBox="true" caption="2riu, resolution 1.700&Aring;" /> '''Alternative models ...)
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Revision as of 09:00, 31 January 2008


2riu, resolution 1.700Å

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Alternative models for two crystal structures of Candida albicans 3,4-dihydroxy-2-butanone 4-phosphate synthase- alternate interpreation

Overview

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.

About this Structure

2RIU is a Single protein structure of sequence from Candida albicans with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

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:15328619

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