1tks: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1tks" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tks, resolution 1.6Å" /> '''Crystal structure of ...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1tks.gif|left|200px]]<br /><applet load="1tks" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1tks.gif|left|200px]]<br /><applet load="1tks" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1tks, resolution 1.6&Aring;" />
caption="1tks, resolution 1.6&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TKS OCA].  
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==
Line 25: Line 25:
[[Category: riboflavin biosynthesis]]
[[Category: riboflavin biosynthesis]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:21:40 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:33 2008''