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| | <StructureSection load='5akq' size='340' side='right'caption='[[5akq]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5akq' size='340' side='right'caption='[[5akq]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5akq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Psesd Psesd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AKQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5akq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._ADP Pseudomonas sp. ADP]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AKQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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]] 2.6Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-isopropylammelide_isopropylaminohydrolase N-isopropylammelide isopropylaminohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.4 3.5.99.4] </span></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=ZN:ZINC+ION'>ZN</scene></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=5akq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5akq OCA], [http://pdbe.org/5akq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5akq RCSB], [http://www.ebi.ac.uk/pdbsum/5akq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5akq 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=5akq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5akq OCA], [https://pdbe.org/5akq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5akq RCSB], [https://www.ebi.ac.uk/pdbsum/5akq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5akq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATZC_PSESD ATZC_PSESD]] Transforms N-isopropylammelide to cyanuric acid and isopropylamine. | + | [https://www.uniprot.org/uniprot/ATZC_PSESD ATZC_PSESD] Transforms N-isopropylammelide to cyanuric acid and isopropylamine. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-isopropylammelide isopropylaminohydrolase]] | + | [[Category: Pseudomonas sp. ADP]] |
| - | [[Category: Psesd]]
| + | [[Category: Balotra S]] |
| - | [[Category: Balotra, S]] | + | [[Category: Briggs LJ]] |
| - | [[Category: Briggs, L J]] | + | [[Category: Newman J]] |
| - | [[Category: Newman, J]] | + | [[Category: Peat TS]] |
| - | [[Category: Peat, T S]] | + | [[Category: Scott C]] |
| - | [[Category: Scott, C]] | + | [[Category: Warden AC]] |
| - | [[Category: Warden, A C]] | + | |
| - | [[Category: Atrazine degradation]]
| + | |
| - | [[Category: Enzyme evolution]]
| + | |
| - | [[Category: Hydrolase]]
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| Structural highlights
Function
ATZC_PSESD Transforms N-isopropylammelide to cyanuric acid and isopropylamine.
Publication Abstract from PubMed
The N-isopropylammelide isopropylaminohydrolase from Pseudomonas sp. strain ADP, AtzC, provides the third hydrolytic step in the mineralization of s-triazine herbicides, such as atrazine. We obtained the X-ray crystal structure of AtzC at 1.84 A with a weak inhibitor bound in the active site and then used a combination of in silico docking and site-directed mutagenesis to understand the interactions between AtzC and its substrate, isopropylammelide. The substitution of an active site histidine residue (His249) for an alanine abolished the enzyme's catalytic activity. We propose a plausible catalytic mechanism, consistent with the biochemical and crystallographic data obtained that is similar to that found in carbonic anhydrase and other members of subtype III of the amidohydrolase family.
X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC.,Balotra S, Warden AC, Newman J, Briggs LJ, Scott C, Peat TS PLoS One. 2015 Sep 21;10(9):e0137700. doi: 10.1371/journal.pone.0137700., eCollection 2015. PMID:26390431[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Balotra S, Warden AC, Newman J, Briggs LJ, Scott C, Peat TS. X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC. PLoS One. 2015 Sep 21;10(9):e0137700. doi: 10.1371/journal.pone.0137700., eCollection 2015. PMID:26390431 doi:http://dx.doi.org/10.1371/journal.pone.0137700
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