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| | <StructureSection load='5k8p' size='340' side='right'caption='[[5k8p]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5k8p' size='340' side='right'caption='[[5k8p]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k8p]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Brasz Brasz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K8P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5K8P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k8p]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_sp. Bradyrhizobium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K8P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6R8:(6~{R})-6-AZANYL-3-NITRO-6-OXIDANYL-CYCLOHEXA-1,3-DIENE-1-CARBOXYLIC+ACID'>6R8</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k8m|5k8m]], [[5k8n|5k8n]], [[5k8o|5k8o]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6R8:(6~{R})-6-AZANYL-3-NITRO-6-OXIDANYL-CYCLOHEXA-1,3-DIENE-1-CARBOXYLIC+ACID'>6R8</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">naaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=376 BRASZ])</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=5k8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k8p OCA], [https://pdbe.org/5k8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k8p RCSB], [https://www.ebi.ac.uk/pdbsum/5k8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k8p 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/5-nitroanthranilic_acid_aminohydrolase 5-nitroanthranilic acid aminohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.8 3.5.99.8] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5k8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k8p OCA], [http://pdbe.org/5k8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k8p RCSB], [http://www.ebi.ac.uk/pdbsum/5k8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k8p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NAAA_BRASZ NAAA_BRASZ]] Catalyzes the deamination of 5-nitroanthranilate (5NAA) to 5-nitrosalicylate (5NSA), the first step in biodegradation of 5-nitroanthranilate.<ref>PMID:20081004</ref> <ref>PMID:21498645</ref> | + | [https://www.uniprot.org/uniprot/NAAA_BRASZ NAAA_BRASZ] Catalyzes the deamination of 5-nitroanthranilate (5NAA) to 5-nitrosalicylate (5NSA), the first step in biodegradation of 5-nitroanthranilate.<ref>PMID:20081004</ref> <ref>PMID:21498645</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: 5-nitroanthranilic acid aminohydrolase]] | + | [[Category: Bradyrhizobium sp]] |
| - | [[Category: Brasz]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kalyoncu, S]] | + | [[Category: Kalyoncu S]] |
| - | [[Category: Deaminase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metalloenzyme]]
| + | |
| - | [[Category: Nitroaromatic]]
| + | |
| Structural highlights
Function
NAAA_BRASZ Catalyzes the deamination of 5-nitroanthranilate (5NAA) to 5-nitrosalicylate (5NSA), the first step in biodegradation of 5-nitroanthranilate.[1] [2]
Publication Abstract from PubMed
Nitroaromatic compounds are typically toxic and resistant to degradation. Bradyrhizobium species strain JS329 metabolizes 5-nitroanthranilic acid (5NAA), which is a molecule secreted by Streptomyces scabies, the plant pathogen responsible for potato scab. The first biodegradation enzyme is 5NAA-aminohydrolase (5NAA-A), a metalloprotease family member that converts 5NAA to 5-nitrosalicylic acid. We characterized 5NAA-A biochemically and obtained snapshots of its mechanism. 5NAA-A, an octamer that can use several divalent transition metals for catalysis in vitro, employs a nucleophilic aromatic substitution mechanism. Unexpectedly, the metal in 5NAA-A is labile but is readily loaded in the presence of substrate. 5NAA-A is specific for 5NAA and cannot hydrolyze other tested derivatives, which are likewise poor inhibitors. The 5NAA-A structure and mechanism expand our understanding of the chemical ecology of an agriculturally important plant and pathogen, and will inform bioremediation and biocatalytic approaches to mitigate the environmental and ecological impact of nitroanilines and other challenging substrates.
Enzymatic hydrolysis by transition-metal-dependent nucleophilic aromatic substitution.,Kalyoncu S, Heaner DP Jr, Kurt Z, Bethel CM, Ukachukwu CU, Chakravarthy S, Spain JC, Lieberman RL Nat Chem Biol. 2016 Oct 3. doi: 10.1038/nchembio.2191. PMID:27694799[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qu Y, Spain JC. Biodegradation of 5-nitroanthranilic acid by Bradyrhizobium sp. strain JS329. Appl Environ Microbiol. 2010 Mar;76(5):1417-22. doi: 10.1128/AEM.02816-09. Epub, 2010 Jan 15. PMID:20081004 doi:http://dx.doi.org/10.1128/AEM.02816-09
- ↑ Qu Y, Spain JC. Molecular and biochemical characterization of the 5-nitroanthranilic acid degradation pathway in Bradyrhizobium sp. strain JS329. J Bacteriol. 2011 Jun;193(12):3057-63. doi: 10.1128/JB.01188-10. Epub 2011 Apr, 15. PMID:21498645 doi:http://dx.doi.org/10.1128/JB.01188-10
- ↑ Kalyoncu S, Heaner DP Jr, Kurt Z, Bethel CM, Ukachukwu CU, Chakravarthy S, Spain JC, Lieberman RL. Enzymatic hydrolysis by transition-metal-dependent nucleophilic aromatic substitution. Nat Chem Biol. 2016 Oct 3. doi: 10.1038/nchembio.2191. PMID:27694799 doi:http://dx.doi.org/10.1038/nchembio.2191
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