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| | <StructureSection load='2v6s' size='340' side='right'caption='[[2v6s]], [[Resolution|resolution]] 2.22Å' scene=''> | | <StructureSection load='2v6s' size='340' side='right'caption='[[2v6s]], [[Resolution|resolution]] 2.22Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v6s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii_rh Toxoplasma gondii rh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V6S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v6s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii_RH Toxoplasma gondii RH]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V6S FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2v6t|2v6t]]</div></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]] 2.22Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4a-hydroxytetrahydrobiopterin_dehydratase 4a-hydroxytetrahydrobiopterin dehydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.96 4.2.1.96] </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=2v6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6s OCA], [https://pdbe.org/2v6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v6s RCSB], [https://www.ebi.ac.uk/pdbsum/2v6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v6s ProSAT]</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=2v6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v6s OCA], [https://pdbe.org/2v6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v6s RCSB], [https://www.ebi.ac.uk/pdbsum/2v6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v6s ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q2Q449_TOXGO Q2Q449_TOXGO] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4a-hydroxytetrahydrobiopterin dehydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Toxoplasma gondii rh]] | + | [[Category: Toxoplasma gondii RH]] |
| - | [[Category: Cameron, S]] | + | [[Category: Cameron S]] |
| - | [[Category: Fyffe, S A]] | + | [[Category: Fyffe SA]] |
| - | [[Category: Hunter, W N]] | + | [[Category: Hunter WN]] |
| - | [[Category: Dehydratase]]
| + | |
| - | [[Category: Enzyme]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Pterin]]
| + | |
| - | [[Category: Toxoplasma]]
| + | |
| Structural highlights
Function
Q2Q449_TOXGO
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The enzyme pterin-4a-carbinolamine dehydratase (PCD) is important for the recycling of pterins within eukaryotic cells. A recombinant expression system for PCD from the apicomplexan parasite Toxoplasma gondii has been prepared, the protein purified and crystallised. Single crystal X-ray diffraction methods have produced a high-resolution structure (1.6A) of the apo-enzyme and a low-resolution structure (3.1A) of a complex with a substrate-like ligand dihydrobiopterin (BH(2)). Analysis of the hydrogen bonding interactions that contribute to binding BH(2) suggest that the ligand is present in an enol tautomeric state, which makes it more similar to the physiological substrate. The enzyme can process (R)- and (S)-forms of pterin-4a-carbinolamine and the ligand complex suggests that His61 and His79 are placed to act independently as general bases for catalysis of the individual enantiomers. Comparisons with orthologues from other protozoan parasites (Plasmodium falciparum and Leishmania major) and with rat PCD, for which the structure is known, indicate a high degree of sequence and structure conservation of this enzyme. The molecular determinants of ligand recognition and PCD reactivity are therefore highly conserved across species.
Crystal structures of Toxoplasma gondii pterin-4a-carbinolamine dehydratase and comparisons with mammalian and parasite orthologues.,Cameron S, Fyffe SA, Goldie S, Hunter WN Mol Biochem Parasitol. 2008 Apr;158(2):131-8. Epub 2007 Dec 15. PMID:18215430[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cameron S, Fyffe SA, Goldie S, Hunter WN. Crystal structures of Toxoplasma gondii pterin-4a-carbinolamine dehydratase and comparisons with mammalian and parasite orthologues. Mol Biochem Parasitol. 2008 Apr;158(2):131-8. Epub 2007 Dec 15. PMID:18215430 doi:10.1016/j.molbiopara.2007.12.002
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