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| | <StructureSection load='6buq' size='340' side='right'caption='[[6buq]], [[Resolution|resolution]] 1.88Å' scene=''> | | <StructureSection load='6buq' size='340' side='right'caption='[[6buq]], [[Resolution|resolution]] 1.88Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6buq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Moota Moota]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BUQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6buq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorella_thermoacetica_ATCC_39073 Moorella thermoacetica ATCC 39073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BUQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR8:BARBITURIC+ACID'>BR8</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PDO:1,3-PROPANDIOL'>PDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.88Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Moth_2120 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264732 MOOTA])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR8:BARBITURIC+ACID'>BR8</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PDO:1,3-PROPANDIOL'>PDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyanuric_acid_amidohydrolase Cyanuric acid amidohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.15 3.5.2.15] </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=6buq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6buq OCA], [https://pdbe.org/6buq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6buq RCSB], [https://www.ebi.ac.uk/pdbsum/6buq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6buq 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=6buq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6buq OCA], [http://pdbe.org/6buq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6buq RCSB], [http://www.ebi.ac.uk/pdbsum/6buq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6buq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAH_MOOTA CAH_MOOTA]] Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret.[HAMAP-Rule:MF_01989]<ref>PMID:19767460</ref> <ref>PMID:28235873</ref> | + | [https://www.uniprot.org/uniprot/CAH_MOOTA CAH_MOOTA] Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret.[HAMAP-Rule:MF_01989]<ref>PMID:19767460</ref> <ref>PMID:28235873</ref> |
| | <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: Cyanuric acid amidohydrolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Moota]] | + | [[Category: Moorella thermoacetica ATCC 39073]] |
| - | [[Category: Aihara, H]] | + | [[Category: Aihara H]] |
| - | [[Category: Shi, K]] | + | [[Category: Shi K]] |
| - | [[Category: Cyanuric acid hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
6buq is a 4 chain structure with sequence from Moorella thermoacetica ATCC 39073. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.88Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CAH_MOOTA Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret.[HAMAP-Rule:MF_01989][1] [2]
Publication Abstract from PubMed
An ancient enzyme family responsible for the catabolism of the prebiotic chemical cyanuric acid (1,3,5-triazine-2,4,6-triol) was recently discovered and is undergoing proliferation in the modern world due to industrial synthesis and dissemination of 1,3,5-triazine compounds. Cyanuric acid has a highly stabilized ring system such that bacteria require a unique enzyme with a novel fold and subtle active site construction to open the ring. Each cyanuric acid hydrolase monomer consists of three isostructural domains that coordinate and activate the three-fold symmetric substrate cyanuric acid for ring opening. We have now solved a series of X-ray structures of an engineered, thermostable cyanuric acid ring-opening enzyme at 1.51 ~ 2.25 A resolution, including various complexes with the substrate, a tight-binding inhibitor, or an analog of the reaction intermediate. These structures reveal asymmetric interactions between the enzyme and bound ligands, a metal ion binding coupled to conformational changes and substrate binding important for enzyme stability, and distinct roles of the isostructural domains of the enzyme. The multiple conformations of the enzyme observed across a series of structures and corroborating biochemical data suggest importance of the structural dynamics in facilitating the substrate entry and the ring-opening reaction, catalyzed by a conserved Ser-Lys dyad.
Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.,Shi K, Cho S, Aukema KG, Lee T, Bera AK, Seffernick JL, Wackett LP, Aihara H PLoS One. 2019 Jun 10;14(6):e0216979. doi: 10.1371/journal.pone.0216979., eCollection 2019. PMID:31181074[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li Q, Seffernick JL, Sadowsky MJ, Wackett LP. Thermostable cyanuric acid hydrolase from Moorella thermoacetica ATCC 39073. Appl Environ Microbiol. 2009 Nov;75(22):6986-91. doi: 10.1128/AEM.01605-09. Epub , 2009 Sep 18. PMID:19767460 doi:http://dx.doi.org/10.1128/AEM.01605-09
- ↑ Peat TS, Balotra S, Wilding M, Hartley CJ, Newman J, Scott C. High resolution X-ray structures of two functionally distinct members of the cyclic amide hydrolase (CyAH) family of Toblerone fold enzymes. Appl Environ Microbiol. 2017 Feb 24. pii: AEM.03365-16. doi:, 10.1128/AEM.03365-16. PMID:28235873 doi:http://dx.doi.org/10.1128/AEM.03365-16
- ↑ Shi K, Cho S, Aukema KG, Lee T, Bera AK, Seffernick JL, Wackett LP, Aihara H. Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis. PLoS One. 2019 Jun 10;14(6):e0216979. doi: 10.1371/journal.pone.0216979., eCollection 2019. PMID:31181074 doi:http://dx.doi.org/10.1371/journal.pone.0216979
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