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| | ==Crystal structure of a 6-pyruvoyltetrahydropterin synthase homologue from Esherichia coli== | | ==Crystal structure of a 6-pyruvoyltetrahydropterin synthase homologue from Esherichia coli== |
| - | <StructureSection load='3qn9' size='340' side='right' caption='[[3qn9]], [[Resolution|resolution]] 2.93Å' scene=''> | + | <StructureSection load='3qn9' size='340' side='right'caption='[[3qn9]], [[Resolution|resolution]] 2.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qn9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QN9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qn9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QN9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.93Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EcDH1_0923 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=469008 ECOBD])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6-pyruvoyltetrahydropterin_synthase 6-pyruvoyltetrahydropterin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.12 4.2.3.12] </span></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=3qn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qn9 OCA], [https://pdbe.org/3qn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qn9 RCSB], [https://www.ebi.ac.uk/pdbsum/3qn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qn9 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qn9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qn9 RCSB], [http://www.ebi.ac.uk/pdbsum/3qn9 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == 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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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3qn9" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 6-pyruvoyltetrahydropterin synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Ecobd]]
| + | [[Category: Lee KH]] |
| - | [[Category: Lee, K H]] | + | [[Category: Seo KH]] |
| - | [[Category: Seo, K H]] | + | [[Category: Zhuang NN]] |
| - | [[Category: Zhuang, N N]] | + | |
| - | [[Category: Bh4 synthase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Zn]]
| + | |
| Structural highlights
Function
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.
Publication Abstract from PubMed
Escherichia coli 6-carboxytetrahydropterin synthase (eCTPS), a homologue of 6-pyruvoyltetrahydropterin synthase (PTPS), possesses a much stronger catalytic activity to cleave the side chain of sepiapterin in vitro compared with genuine PTPS activity and catalyzes the conversion of dihydroneopterin triphosphate to 6-carboxy-5,6,7,8-tetrahydropterin in vivo. Crystal structures of wild-type apo eCTPS and of a Cys27Ala mutant eCTPS complexed with sepiapterin have been determined to 2.3 and 2.5 A resolution, respectively. The structures are highly conserved at the active site and the Zn(2+) binding site. However, comparison of the eCTPS structures with those of mammalian PTPS homologues revealed that two specific residues, Trp51 and Phe55, that are not found in mammalian PTPS keep the substrate bound by stacking it with their side chains. Replacement of these two residues by site-directed mutagenesis to the residues Met and Leu, which are only found in mammalian PTPS, converted eCTPS to the mammalian PTPS activity. These studies confirm that these two aromatic residues in eCTPS play an essential role in stabilizing the substrate and in the specific enzyme activity that differs from the original PTPS activity. These aromatic residues Trp51 and Phe55 are a key signature of bacterial PTPS enzymes that distinguish them from mammalian PTPS homologues.
Structural basis of a novel activity of bacterial 6-pyruvoyltetrahydropterin synthase homologues distinct from mammalian 6-pyruvoyltetrahydropterin synthase activity.,Seo KH, Zhuang N, Park YS, Park KH, Lee KH Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1212-23. doi:, 10.1107/S1399004714002016. Epub 2014 Apr 26. PMID:24816091[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seo KH, Zhuang N, Park YS, Park KH, Lee KH. Structural basis of a novel activity of bacterial 6-pyruvoyltetrahydropterin synthase homologues distinct from mammalian 6-pyruvoyltetrahydropterin synthase activity. Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1212-23. doi:, 10.1107/S1399004714002016. Epub 2014 Apr 26. PMID:24816091 doi:http://dx.doi.org/10.1107/S1399004714002016
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