|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6izh' size='340' side='right'caption='[[6izh]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6izh' size='340' side='right'caption='[[6izh]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6izh]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Achromobacter_georgiopolitanum Achromobacter georgiopolitanum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IZH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6izh]] is a 9 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=6IZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IZH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.754Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">amnD ([http://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=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-aminomuconate_deaminase 2-aminomuconate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.5 3.5.99.5] </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=6izh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6izh OCA], [https://pdbe.org/6izh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6izh RCSB], [https://www.ebi.ac.uk/pdbsum/6izh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6izh 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=6izh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6izh OCA], [http://pdbe.org/6izh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6izh RCSB], [http://www.ebi.ac.uk/pdbsum/6izh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6izh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AMND_PSESP AMND_PSESP]] Involved in the modified meta-cleavage pathway for the 2-aminophenol catabolism. Only active toward 2-aminomuconic acid.<ref>PMID:9169437</ref> | + | [https://www.uniprot.org/uniprot/AMND_PSESP AMND_PSESP] Involved in the modified meta-cleavage pathway for the 2-aminophenol catabolism. Only active toward 2-aminomuconic acid.<ref>PMID:9169437</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 27: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 2-aminomuconate deaminase]] | |
| - | [[Category: Achromobacter georgiopolitanum]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, Y J]] | + | [[Category: Pseudomonas sp]] |
| - | [[Category: Chen, Y P]] | + | [[Category: Chen YJ]] |
| - | [[Category: Su, D]] | + | [[Category: Chen YP]] |
| - | [[Category: Hexamer]] | + | [[Category: Su D]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
AMND_PSESP Involved in the modified meta-cleavage pathway for the 2-aminophenol catabolism. Only active toward 2-aminomuconic acid.[1]
Publication Abstract from PubMed
The bacterium Pseudomonas species sp. AP-3 is one of several microorganisms that are capable of using 2-aminophenol as its sole source of carbon, nitrogen and energy. Several 2-aminophenol-metabolizing enzymes have pivotal roles in the biodegradation of aniline and its derivatives as environmental pollutants in Pseudomonas. The bacterium Pseudomonas sp. AP-3 recruits a unique 2-aminomuconate deaminase (AmnE) to hydrolyze 2-aminomuconate to 4-oxalocrotonate, and releases ammonia in the modified meta-cleavage pathway by forming various compounds-including acetaldehyde, pyruvic acid, acetyl-CoA, and succinate-that may enter the Krebs cycle. AmnE also belongs to the YjgF/YER057c/UK114 family (also known as the Rid family), which is conserved in all domains of life and prefers structurally homotrimeric forms with diverse functional purposes. To study the mechanism of the modified meta-cleavage pathway in Pseudomonas sp. AP-3, we determined the first crystal structure of AmnE from Pseudomonas sp. AP-3 at 1.75 A. AmnE forms a unique homohexamer instead of a trimer which is normally adopted by the members of YjgF/YER057c/UK114 family. Based on the structure of the AmnE hexamer, we observed a hydrophobic base composed of six Lp3 loops (residues 122-131) in each of the AmnE protomers that have pivotal roles in the assembly of the hexamer. Eighteen hydrogen bonds formed by the residues Met(96), Pro(126), and Arg(56), which surround the hydrophobic base, allowed the combination of the two trimers into a stable hexamer. The single mutant of AmnE R56A lost the ability to maintain the hexameric conformation, and revealed that the hydrogen bonds between residues Arg(56) and Met(96) have pivotal roles in the AmnE hexameric assembly.
A Unique Homo-Hexameric Structure of 2-Aminomuconate Deaminase in the Bacterium Pseudomonas species AP-3.,Chen Y, Chen Y, Jiang H, Lu D, Hu T, Bi G, Ran Y, Yu B, Dong H, Su D Front Microbiol. 2019 Sep 6;10:2079. doi: 10.3389/fmicb.2019.02079. eCollection, 2019. PMID:31555255[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Chen Y, Chen Y, Jiang H, Lu D, Hu T, Bi G, Ran Y, Yu B, Dong H, Su D. A Unique Homo-Hexameric Structure of 2-Aminomuconate Deaminase in the Bacterium Pseudomonas species AP-3. Front Microbiol. 2019 Sep 6;10:2079. doi: 10.3389/fmicb.2019.02079. eCollection, 2019. PMID:31555255 doi:http://dx.doi.org/10.3389/fmicb.2019.02079
|
