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| | <StructureSection load='4v1x' size='340' side='right'caption='[[4v1x]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4v1x' size='340' side='right'caption='[[4v1x]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v1x]] is a 6 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=4V1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V1X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v1x]] is a 6 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=4V1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V1X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v1y|4v1y]]</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=4v1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v1x OCA], [https://pdbe.org/4v1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v1x RCSB], [https://www.ebi.ac.uk/pdbsum/4v1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v1x ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Atrazine_chlorohydrolase Atrazine chlorohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.8 3.8.1.8] </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=4v1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v1x OCA], [http://pdbe.org/4v1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v1x RCSB], [http://www.ebi.ac.uk/pdbsum/4v1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v1x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATZA_PSESD ATZA_PSESD]] Hydrolytically dechlorinates atrazine to hydroxyatrazine. Dechlorinates also simazine, and desethylatrazine but is not active with melamine, terbutylazine, or desethyldesisopropylatrazine.<ref>PMID:8759853</ref> | + | [https://www.uniprot.org/uniprot/ATZA_PSESD ATZA_PSESD] Hydrolytically dechlorinates atrazine to hydroxyatrazine. Dechlorinates also simazine, and desethylatrazine but is not active with melamine, terbutylazine, or desethyldesisopropylatrazine.<ref>PMID:8759853</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: Atrazine chlorohydrolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Psesd]] | + | [[Category: Pseudomonas sp. ADP]] |
| - | [[Category: Balotra, S]] | + | [[Category: Balotra S]] |
| - | [[Category: Lucent, D]] | + | [[Category: Lucent D]] |
| - | [[Category: Newman, J]] | + | [[Category: Newman J]] |
| - | [[Category: Peat, T S]] | + | [[Category: Peat TS]] |
| - | [[Category: Scott, C]] | + | [[Category: Scott C]] |
| - | [[Category: Warden, A C]] | + | [[Category: Warden AC]] |
| - | [[Category: Bioremediation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protein evolution]]
| + | |
| Structural highlights
Function
ATZA_PSESD Hydrolytically dechlorinates atrazine to hydroxyatrazine. Dechlorinates also simazine, and desethylatrazine but is not active with melamine, terbutylazine, or desethyldesisopropylatrazine.[1]
Publication Abstract from PubMed
Atrazine chlorohydrolase (AtzA) was discovered and purified in the early 1990s from soil that had been exposed to the widely used herbicide atrazine. It was subsequently found that this enzyme catalyzes the first and necessary step in the breakdown of atrazine by the soil organism Pseudomonas sp. strain ADP. Although it has taken 20 years, a crystal structure of the full hexameric form of AtzA has now been obtained. AtzA is less well adapted to its physiological role (i.e. atrazine dechlorination) than the alternative metal-dependent atrazine chlorohydrolase (TrzN), with a substrate-binding pocket that is under considerable strain and for which the substrate is a poor fit.
The structure of the hexameric atrazine chlorohydrolase AtzA.,Peat TS, Newman J, Balotra S, Lucent D, Warden AC, Scott C Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):710-20. doi:, 10.1107/S1399004715000619. Epub 2015 Feb 26. PMID:25760618[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ de Souza ML, Sadowsky MJ, Wackett LP. Atrazine chlorohydrolase from Pseudomonas sp. strain ADP: gene sequence, enzyme purification, and protein characterization. J Bacteriol. 1996 Aug;178(16):4894-900. PMID:8759853
- ↑ Peat TS, Newman J, Balotra S, Lucent D, Warden AC, Scott C. The structure of the hexameric atrazine chlorohydrolase AtzA. Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):710-20. doi:, 10.1107/S1399004715000619. Epub 2015 Feb 26. PMID:25760618 doi:http://dx.doi.org/10.1107/S1399004715000619
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