1ovm: Difference between revisions
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New page: left|200px<br /><applet load="1ovm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ovm, resolution 2.65Å" /> '''Crystal structure of... |
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[[Image:1ovm.jpg|left|200px]]<br /><applet load="1ovm" size=" | [[Image:1ovm.jpg|left|200px]]<br /><applet load="1ovm" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ovm, resolution 2.65Å" /> | caption="1ovm, resolution 2.65Å" /> | ||
'''Crystal structure of Indolepyruvate decarboxylase from Enterobacter cloacae'''<br /> | '''Crystal structure of Indolepyruvate decarboxylase from Enterobacter cloacae'''<br /> | ||
==Overview== | ==Overview== | ||
The thiamin diphosphate-dependent enzyme indolepyruvate decarboxylase | The thiamin diphosphate-dependent enzyme indolepyruvate decarboxylase catalyses the formation of indoleacetaldehyde from indolepyruvate, one step in the indolepyruvate pathway of biosynthesis of the plant hormone indole-3-acetic acid. The crystal structure of this enzyme from Enterobacter cloacae has been determined at 2.65 A resolution and refined to a crystallographic R-factor of 20.5% (Rfree 23.6%). The subunit of indolepyruvate decarboxylase contains three domains of open alpha/beta topology, which are similar in structure to that of pyruvate decarboxylase. The tetramer has pseudo 222 symmetry and can be described as a dimer of dimers. It resembles the tetramer of pyruvate decarboxylase from Zymomonas mobilis, but with a relative difference of 20 degrees in the angle between the two dimers. Active site residues are highly conserved in indolepyruvate/pyruvate decarboxylase, suggesting that the interactions with the cofactor thiamin diphosphate and the catalytic mechanisms are very similar. The substrate binding site in indolepyruvate decarboxylase contains a large hydrophobic pocket which can accommodate the bulky indole moiety of the substrate. In pyruvate decarboxylases this pocket is smaller in size and allows discrimination of larger vs. smaller substrates. In most pyruvate decarboxylases, restriction of cavity size is due to replacement of residues at three positions by large, hydrophobic amino acids such as tyrosine or tryptophan. | ||
==About this Structure== | ==About this Structure== | ||
1OVM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae] with MG and TPP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Indolepyruvate_decarboxylase Indolepyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.74 4.1.1.74] Full crystallographic information is available from [http:// | 1OVM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae] 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/Indolepyruvate_decarboxylase Indolepyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.74 4.1.1.74] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: thiamine diphosphate]] | [[Category: thiamine diphosphate]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:01 2008'' | ||