2g1i
From Proteopedia
(New page: 200px<br /><applet load="2g1i" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g1i, resolution 2.260Å" /> '''Crystal Structure o...) |
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| - | [[Image:2g1i.jpg|left|200px]]<br /><applet load="2g1i" size=" | + | [[Image:2g1i.jpg|left|200px]]<br /><applet load="2g1i" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2g1i, resolution 2.260Å" /> | caption="2g1i, resolution 2.260Å" /> | ||
'''Crystal Structure of Pyruvate Decarboxylase from Kluyveromyces lactis'''<br /> | '''Crystal Structure of Pyruvate Decarboxylase from Kluyveromyces lactis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis | + | The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis has been determined to 2.26 A resolution. Like other yeast enzymes, Kluyveromyces lactis pyruvate decarboxylase is subject to allosteric substrate activation. Binding of substrate at a regulatory site induces catalytic activity. This process is accompanied by conformational changes and subunit rearrangements. In the nonactivated form of the corresponding enzyme from Saccharomyces cerevisiae, all active sites are solvent accessible due to the high flexibility of loop regions 106-113 and 292-301. The binding of the activator pyruvamide arrests these loops. Consequently, two of four active sites become closed. In Kluyveromyces lactis pyruvate decarboxylase, this half-side closed tetramer is present even without any activator. However, one of the loops (residues 105-113), which are flexible in nonactivated Saccharomyces cerevisiae pyruvate decarboxylase, remains flexible. Even though the tetramer assemblies of both enzyme species are different in the absence of activating agents, their substrate activation kinetics are similar. This implies an equilibrium between the open and the half-side closed state of yeast pyruvate decarboxylase tetramers. The completely open enzyme state is favoured for Saccharomyces cerevisiae pyruvate decarboxylase, whereas the half-side closed form is predominant for Kluyveromyces lactis pyruvate decarboxylase. Consequently, the structuring of the flexible loop region 105-113 seems to be the crucial step during the substrate activation process of Kluyveromyces lactis pyruvate decarboxylase. |
==About this Structure== | ==About this Structure== | ||
| - | 2G1I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis] with MG and TPP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] Full crystallographic information is available from [http:// | + | 2G1I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis] 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/Pyruvate_decarboxylase Pyruvate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.1 4.1.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G1I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kutter, S.]] | [[Category: Kutter, S.]] | ||
[[Category: Relle, S.]] | [[Category: Relle, S.]] | ||
| - | [[Category: Weiss, M | + | [[Category: Weiss, M S.]] |
[[Category: Wille, G.]] | [[Category: Wille, G.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: substrate activation]] | [[Category: substrate activation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:13 2008'' |
Revision as of 15:27, 21 February 2008
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Crystal Structure of Pyruvate Decarboxylase from Kluyveromyces lactis
Overview
The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis has been determined to 2.26 A resolution. Like other yeast enzymes, Kluyveromyces lactis pyruvate decarboxylase is subject to allosteric substrate activation. Binding of substrate at a regulatory site induces catalytic activity. This process is accompanied by conformational changes and subunit rearrangements. In the nonactivated form of the corresponding enzyme from Saccharomyces cerevisiae, all active sites are solvent accessible due to the high flexibility of loop regions 106-113 and 292-301. The binding of the activator pyruvamide arrests these loops. Consequently, two of four active sites become closed. In Kluyveromyces lactis pyruvate decarboxylase, this half-side closed tetramer is present even without any activator. However, one of the loops (residues 105-113), which are flexible in nonactivated Saccharomyces cerevisiae pyruvate decarboxylase, remains flexible. Even though the tetramer assemblies of both enzyme species are different in the absence of activating agents, their substrate activation kinetics are similar. This implies an equilibrium between the open and the half-side closed state of yeast pyruvate decarboxylase tetramers. The completely open enzyme state is favoured for Saccharomyces cerevisiae pyruvate decarboxylase, whereas the half-side closed form is predominant for Kluyveromyces lactis pyruvate decarboxylase. Consequently, the structuring of the flexible loop region 105-113 seems to be the crucial step during the substrate activation process of Kluyveromyces lactis pyruvate decarboxylase.
About this Structure
2G1I is a Single protein structure of sequence from Kluyveromyces lactis with and as ligands. Active as Pyruvate decarboxylase, with EC number 4.1.1.1 Full crystallographic information is available from OCA.
Reference
The crystal structure of pyruvate decarboxylase from Kluyveromyces lactis. Implications for the substrate activation mechanism of this enzyme., Kutter S, Wille G, Relle S, Weiss MS, Hubner G, Konig S, FEBS J. 2006 Sep;273(18):4199-209. PMID:16939618
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