1tks
From Proteopedia
(New page: 200px<br /><applet load="1tks" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tks, resolution 1.6Å" /> '''Crystal structure of ...) |
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| - | [[Image:1tks.gif|left|200px]]<br /><applet load="1tks" size=" | + | [[Image:1tks.gif|left|200px]]<br /><applet load="1tks" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tks, resolution 1.6Å" /> | caption="1tks, resolution 1.6Å" /> | ||
'''Crystal structure of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans'''<br /> | '''Crystal structure of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A synthetic gene specifying a putative 3,4-dihydroxy-2-butanone | + | 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== | ==About this Structure== | ||
| - | 1TKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans_sc5314 Candida albicans sc5314]. Full crystallographic information is available from [http:// | + | 1TKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans_sc5314 Candida albicans sc5314]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TKS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: riboflavin biosynthesis]] | [[Category: riboflavin biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:33 2008'' |
Revision as of 13:14, 21 February 2008
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Crystal structure of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans
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
1TKS 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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