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| | <StructureSection load='7bzv' size='340' side='right'caption='[[7bzv]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='7bzv' size='340' side='right'caption='[[7bzv]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7bzv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_georgiopolitanum Achromobacter georgiopolitanum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BZV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bzv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BZV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.988Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">amnC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Achromobacter georgiopolitanum])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aminomuconate-semialdehyde_dehydrogenase Aminomuconate-semialdehyde dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.32 1.2.1.32] </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=7bzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bzv OCA], [https://pdbe.org/7bzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bzv RCSB], [https://www.ebi.ac.uk/pdbsum/7bzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bzv 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=7bzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bzv OCA], [https://pdbe.org/7bzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bzv RCSB], [https://www.ebi.ac.uk/pdbsum/7bzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bzv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/AMNC_PSESP AMNC_PSESP]] Involved in the modified meta-cleavage pathway for 2-aminophenol catabolism. The enzyme is also active toward 2-hydroxymuconic 6-semialdehyde, acetaldehyde, propionaldehyde, and butyraldehyde.<ref>PMID:9169437</ref>
| + | [https://www.uniprot.org/uniprot/AMNC_PSESP AMNC_PSESP] Involved in the modified meta-cleavage pathway for 2-aminophenol catabolism. The enzyme is also active toward 2-hydroxymuconic 6-semialdehyde, acetaldehyde, propionaldehyde, and butyraldehyde.<ref>PMID:9169437</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: Achromobacter georgiopolitanum]] | |
| - | [[Category: Aminomuconate-semialdehyde dehydrogenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, Y J]] | + | [[Category: Pseudomonas sp]] |
| - | [[Category: Shi, Q L]] | + | [[Category: Chen YJ]] |
| - | [[Category: Su, D]] | + | [[Category: Shi QL]] |
| - | [[Category: Biosynthetic protein]] | + | [[Category: Su D]] |
| - | [[Category: Meta-cleavage pathway for 2-aminophenol catabolism. 2-aminomuconic 6-semialdehyde dehydrogenase]]
| + | |
| Structural highlights
Function
AMNC_PSESP Involved in the modified meta-cleavage pathway for 2-aminophenol catabolism. The enzyme is also active toward 2-hydroxymuconic 6-semialdehyde, acetaldehyde, propionaldehyde, and butyraldehyde.[1]
Publication Abstract from PubMed
The bacterium Pseudomonas sp. AP-3 is able to use the environmental pollutant 2-aminophenol as its sole source of carbon, nitrogen, and energy. Eight genes (amnA, B, C, D, E, F, G, and H) encoding 2-aminophenol metabolizing enzymes are clustered into a single operon. 2-Aminomuconic 6-semialdehyde dehydrogenase (AmnC), a member of the aldehyde dehydrogenase (ALDH) superfamily, is responsible for oxidizing 2-aminomuconic 6-semialdehyde to 2-aminomuconate. In contrast to many other members of the ALDH superfamily, the structural basis of the catalytic activity of AmnC remains elusive. Here, we present the crystal structure of AmnC, which displays a homotetrameric quaternary assembly that is directly involved in its enzymatic activity. The tetrameric state of AmnC in solution was also presented using small-angle X-ray scattering. The tetramerization of AmnC is mediated by the assembly of a protruding hydrophobic beta-strand motif and residues V121 and S123 located in the NAD(+) -binding domain of each subunit. Dimeric mutants of AmnC dramatically lose NAD(+) binding affinity and failed to oxidize the substrate analogue 2-hydroxymuconate-6-semialdehyde to alpha-hydroxymuconic acid, indicating that tetrameric assembly of AmnC is functional requirement.
The tetrameric assembly of 2-aminomuconic 6-semialdehyde dehydrogenase is a functional requirement of cofactor NAD(+) binding.,Shi Q, Chen Y, Li X, Dong H, Chen C, Zhong Z, Yang C, Liu G, Su D Environ Microbiol. 2021 Nov 22. doi: 10.1111/1462-2920.15840. PMID:34806815[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takenaka S, Murakami S, Shinke R, Hatakeyama K, Yukawa H, Aoki K. Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme. J Biol Chem. 1997 Jun 6;272(23):14727-32. PMID:9169437
- ↑ Shi Q, Chen Y, Li X, Dong H, Chen C, Zhong Z, Yang C, Liu G, Su D. The tetrameric assembly of 2-aminomuconic 6-semialdehyde dehydrogenase is a functional requirement of cofactor NAD(+) binding. Environ Microbiol. 2021 Nov 22. doi: 10.1111/1462-2920.15840. PMID:34806815 doi:http://dx.doi.org/10.1111/1462-2920.15840
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