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==X-ray structure of phenylpyruvate decarboxylase in complex with 2-(1-hydroxyethyl)-3-deaza-ThDP== | |||
<StructureSection load='2q5l' size='340' side='right'caption='[[2q5l]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2q5l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Azospirillum_brasilense Azospirillum brasilense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q5L FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | |||
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=R1T:2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-[(1R)-1-HYDROXYETHYL]-3-METHYL-2-THIENYL}ETHYL+TRIHYDROGEN+DIPHOSPHATE'>R1T</scene>, <scene name='pdbligand=S1T:2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-[(1S)-1-HYDROXYETHYL]-3-METHYL-2-THIENYL}ETHYL+TRIHYDROGEN+DIPHOSPHATE'>S1T</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q5l OCA], [https://pdbe.org/2q5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q5l RCSB], [https://www.ebi.ac.uk/pdbsum/2q5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q5l ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DCIP_AZOBR DCIP_AZOBR] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q5/2q5l_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2q5l ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:17905741</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2q5l" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Phenylpyruvate decarboxylase|Phenylpyruvate decarboxylase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[Category: Azospirillum brasilense]] | [[Category: Azospirillum brasilense]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Leeper FJ]] | |||
[[Category: Leeper | [[Category: Spaepen S]] | ||
[[Category: Spaepen | [[Category: Steyaert J]] | ||
[[Category: Steyaert | [[Category: Vanderleyden J]] | ||
[[Category: Vanderleyden | [[Category: Versees W]] | ||
[[Category: Versees | [[Category: Wood MD]] | ||
[[Category: Wood | |||
Latest revision as of 14:22, 30 August 2023
X-ray structure of phenylpyruvate decarboxylase in complex with 2-(1-hydroxyethyl)-3-deaza-ThDPX-ray structure of phenylpyruvate decarboxylase in complex with 2-(1-hydroxyethyl)-3-deaza-ThDP
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThiamine 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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