1itz

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(New page: 200px<br /><applet load="1itz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1itz, resolution 2.3&Aring;" /> '''Maize Transketolase i...)
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[[Image:1itz.gif|left|200px]]<br /><applet load="1itz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1itz, resolution 2.3&Aring;" />
caption="1itz, resolution 2.3&Aring;" />
'''Maize Transketolase in complex with TPP'''<br />
'''Maize Transketolase in complex with TPP'''<br />
==Overview==
==Overview==
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The gene specifying plastid transketolase (TK) of maize (Zea mays) was, cloned from a cDNA library by southern blotting using a heterologous probe, from sorghum (Sorghum bicolor). A recombinant fusion protein comprising, thioredoxin of Escherichia coli and mature TK of maize was expressed at a, high level in E. coli and cleaved with thrombin, affording plastid TK. The, protein in complex with thiamine pyrophoshate was crystallized, and its, structure was solved by molecular replacement. The enzyme is a C2, symmetric homodimer closely similar to the enzyme from yeast, (Saccharomyces cerevisiae). Each subunit is folded into three domains. The, two topologically equivalent active sites are located in the subunit, interface region and resemble those of the yeast enzyme.
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The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of Escherichia coli and mature TK of maize was expressed at a high level in E. coli and cleaved with thrombin, affording plastid TK. The protein in complex with thiamine pyrophoshate was crystallized, and its structure was solved by molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into three domains. The two topologically equivalent active sites are located in the subunit interface region and resemble those of the yeast enzyme.
==About this Structure==
==About this Structure==
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1ITZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with MG and TPP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transketolase Transketolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ITZ OCA].
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1ITZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=TPP:'>TPP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transketolase Transketolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ITZ OCA].
==Reference==
==Reference==
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[[Category: zea mays]]
[[Category: zea mays]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:39:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:37 2008''

Revision as of 11:15, 21 February 2008

Image:1itz.gif

1itz, resolution 2.3Å

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Maize Transketolase in complex with TPP

Overview

The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of Escherichia coli and mature TK of maize was expressed at a high level in E. coli and cleaved with thrombin, affording plastid TK. The protein in complex with thiamine pyrophoshate was crystallized, and its structure was solved by molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into three domains. The two topologically equivalent active sites are located in the subunit interface region and resemble those of the yeast enzyme.

About this Structure

1ITZ is a Single protein structure of sequence from Zea mays with and as ligands. Active as Transketolase, with EC number 2.2.1.1 Full crystallographic information is available from OCA.

Reference

Structure and properties of an engineered transketolase from maize., Gerhardt S, Echt S, Busch M, Freigang J, Auerbach G, Bader G, Martin WF, Bacher A, Huber R, Fischer M, Plant Physiol. 2003 Aug;132(4):1941-9. PMID:12913150

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