1tku
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= CARib3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237561 Candida albicans SC5314]) | |GENE= CARib3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237561 Candida albicans SC5314]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tku OCA], [http://www.ebi.ac.uk/pdbsum/1tku PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tku RCSB]</span> | ||
}} | }} | ||
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[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Steinbacher, S.]] | [[Category: Steinbacher, S.]] | ||
| - | + | [[Category: 3,4-dihydroxy-2-butanone 4-phosphate synthase]] | |
| - | [[Category: 3 | + | |
| - | + | ||
[[Category: candida albican]] | [[Category: candida albican]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: synthetic gene]] | [[Category: synthetic gene]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:57:27 2008'' |
Revision as of 20:57, 30 March 2008
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| , resolution 1.66Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CARib3 (Candida albicans SC5314) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans in complex with Ribulose-5-phosphate
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
1TKU is a Single protein structure of sequence from Candida albicans sc5314. 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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