4ntn: Difference between revisions
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==E.coli QueD, SeMet protein, 2A resolution== | ==E.coli QueD, SeMet protein, 2A resolution== | ||
<StructureSection load='4ntn' size='340' side='right' caption='[[4ntn]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='4ntn' size='340' side='right'caption='[[4ntn]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ntn]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ntn]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NTN FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand= | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4ntn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ntn OCA], [https://pdbe.org/4ntn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ntn RCSB], [https://www.ebi.ac.uk/pdbsum/4ntn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ntn ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/QUED_ECOLI QUED_ECOLI] Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. Can also convert 6-pyruvoyltetrahydropterin (PPH4) and sepiapterin to CPH4; these 2 compounds are probably intermediates in the reaction from H2NTP. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bandarian | [[Category: Bandarian V]] | ||
[[Category: Miles | [[Category: Miles ZD]] | ||
[[Category: Roberts | [[Category: Roberts SA]] | ||
Revision as of 11:39, 18 January 2023
E.coli QueD, SeMet protein, 2A resolutionE.coli QueD, SeMet protein, 2A resolution
Structural highlights
FunctionQUED_ECOLI Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. Can also convert 6-pyruvoyltetrahydropterin (PPH4) and sepiapterin to CPH4; these 2 compounds are probably intermediates in the reaction from H2NTP. Publication Abstract from PubMed6-Pyruvoyltetrahydropterin synthase (PTPS) homologs in both mammals and bacteria catalyze distinct reactions using the same 7,8-dihydroneopterin triphosphate substrate. The mammalian enzyme converts 7,8-dihydroneopterin triphosphate to 6-pyruvoyltetrahydropterin, whereas the bacterial enzyme catalyzes the formation of 6-carboxy-5,6,7,8-tetrahydropterin. To understand the basis for the differential activities we determined the crystal structure of a bacterial PTPS homolog in the presence and absence of various ligands. Comparison to mammalian structures revealed that although the active sites are nearly structurally identical, the bacterial enzyme houses a His/Asp dyad that is absent from the mammalian protein. Steady state and time-resolved kinetic analysis of the reaction catalyzed by the bacterial homolog revealed that these residues are responsible for the catalytic divergence. This study demonstrates how small variations in the active site can lead to the emergence of new functions in existing protein folds. Biochemical and Structural Studies of 6-Carboxy-5,6,7,8-tetrahydropterin Synthase Reveal the Molecular Basis of Catalytic Promiscuity within the Tunnel-fold Superfamily.,Miles ZD, Roberts SA, McCarty RM, Bandarian V J Biol Chem. 2014 Aug 22;289(34):23641-52. doi: 10.1074/jbc.M114.555680. Epub, 2014 Jul 2. PMID:24990950[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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