2q5o: Difference between revisions
New page: left|200px<br /><applet load="2q5o" size="350" color="white" frame="true" align="right" spinBox="true" caption="2q5o, resolution 2.15Å" /> '''X-ray structure of p... |
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==Overview== | ==Overview== | ||
Thiamine diphosphate-dependent enzymes are involved in a wide variety of | Thiamine diphosphate-dependent enzymes are involved in a wide variety of metabolic pathways. The molecular mechanism behind active site communication and substrate activation, observed in some of these enzymes, has since long been an area of debate. Here, we report the crystal structures of a phenylpyruvate decarboxylase in complex with its substrates and a covalent reaction intermediate analogue. These structures reveal the regulatory site and unveil the mechanism of allosteric substrate activation. This signal transduction relies on quaternary structure reorganizations, domain rotations, and a pathway of local conformational changes that are relayed from the regulatory site to the active site. The current findings thus uncover the molecular mechanism by which the binding of a substrate in the regulatory site is linked to the mounting of the catalytic machinery in the active site in this thiamine diphosphate-dependent enzyme. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase., Versees W, Spaepen S, Wood MD, Leeper FJ, Vanderleyden J, Steyaert J, J Biol Chem. 2007 Sep 28 | Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase., Versees W, Spaepen S, Wood MD, Leeper FJ, Vanderleyden J, Steyaert J, J Biol Chem. 2007 Nov 30;282(48):35269-78. Epub 2007 Sep 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17905741 17905741] | ||
[[Category: Azospirillum brasilense]] | [[Category: Azospirillum brasilense]] | ||
[[Category: Phenylpyruvate decarboxylase]] | [[Category: Phenylpyruvate decarboxylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Leeper, F | [[Category: Leeper, F J.]] | ||
[[Category: Spaepen, S.]] | [[Category: Spaepen, S.]] | ||
[[Category: Steyaert, J.]] | [[Category: Steyaert, J.]] | ||
[[Category: Vanderleyden, J.]] | [[Category: Vanderleyden, J.]] | ||
[[Category: Versees, W.]] | [[Category: Versees, W.]] | ||
[[Category: Wood, M | [[Category: Wood, M D.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: thiamine diphosphate]] | [[Category: thiamine diphosphate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:36:15 2008'' | ||
Revision as of 19:36, 21 February 2008
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X-ray structure of phenylpyruvate decarboxylase in complex with 3-deaza-ThDP and phenylpyruvate
OverviewOverview
Thiamine diphosphate-dependent enzymes are involved in a wide variety of metabolic pathways. The molecular mechanism behind active site communication and substrate activation, observed in some of these enzymes, has since long been an area of debate. Here, we report the crystal structures of a phenylpyruvate decarboxylase in complex with its substrates and a covalent reaction intermediate analogue. These structures reveal the regulatory site and unveil the mechanism of allosteric substrate activation. This signal transduction relies on quaternary structure reorganizations, domain rotations, and a pathway of local conformational changes that are relayed from the regulatory site to the active site. The current findings thus uncover the molecular mechanism by which the binding of a substrate in the regulatory site is linked to the mounting of the catalytic machinery in the active site in this thiamine diphosphate-dependent enzyme.
About this StructureAbout this Structure
2Q5O is a Single protein structure of sequence from Azospirillum brasilense with , , and as ligands. Active as Phenylpyruvate decarboxylase, with EC number 4.1.1.43 Full crystallographic information is available from OCA.
ReferenceReference
Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase., Versees W, Spaepen S, Wood MD, Leeper FJ, Vanderleyden J, Steyaert J, J Biol Chem. 2007 Nov 30;282(48):35269-78. Epub 2007 Sep 28. PMID:17905741
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