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| | ==The Phenylacetyl-CoA monooxygenase PaaAC subcomplex with coenzyme A== | | ==The Phenylacetyl-CoA monooxygenase PaaAC subcomplex with coenzyme A== |
| - | <StructureSection load='3pvy' size='340' side='right' caption='[[3pvy]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='3pvy' size='340' side='right'caption='[[3pvy]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pvy]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PVY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PVY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pvy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PVY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pvr|3pvr]], [[3pvt|3pvt]], [[3pw1|3pw1]], [[3pw8|3pw8]], [[3pwq|3pwq]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1388, JW1383, paaA, ydbO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), b1390, JW1385, paaC, ydbP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3pvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvy OCA], [https://pdbe.org/3pvy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pvy RCSB], [https://www.ebi.ac.uk/pdbsum/3pvy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pvy 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=3pvy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pvy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pvy RCSB], [http://www.ebi.ac.uk/pdbsum/3pvy PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAAA_ECOLI PAAA_ECOLI]] Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit A is the catalytic subunit involved in the incorporation of one atom of molecular oxygen into phenylacetyl-CoA.<ref>PMID:9748275</ref> <ref>PMID:16997993</ref> <ref>PMID:20660314</ref> <ref>PMID:21247899</ref> [[http://www.uniprot.org/uniprot/PAAC_ECOLI PAAC_ECOLI]] Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit C may be essential for structural integrity of the alpha subunit.<ref>PMID:9748275</ref> <ref>PMID:16997993</ref> <ref>PMID:20660314</ref> | + | [https://www.uniprot.org/uniprot/PAAA_ECOLI PAAA_ECOLI] Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit A is the catalytic subunit involved in the incorporation of one atom of molecular oxygen into phenylacetyl-CoA.<ref>PMID:9748275</ref> <ref>PMID:16997993</ref> <ref>PMID:20660314</ref> <ref>PMID:21247899</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3pvy" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Epoxidase 3D structures|Epoxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli str. K-12 substr. MG1655]] |
| - | [[Category: Structural genomic]] | + | [[Category: Large Structures]] |
| - | [[Category: Cygler, M]] | + | [[Category: Cygler M]] |
| - | [[Category: Grishin, A M]] | + | [[Category: Grishin AM]] |
| - | [[Category: Bacterial multicomponent monooxygenase]]
| + | |
| - | [[Category: Bsgi]]
| + | |
| - | [[Category: Ferritin-like fold]]
| + | |
| - | [[Category: Oxidoreductase]]
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| - | [[Category: Protein-protein complex]]
| + | |
| Structural highlights
Function
PAAA_ECOLI Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit A is the catalytic subunit involved in the incorporation of one atom of molecular oxygen into phenylacetyl-CoA.[1] [2] [3] [4]
Publication Abstract from PubMed
The utilization of phenylacetic acid (PA) in Escherichia coli occurs through a hybrid pathway that shows features of both aerobic and anaerobic metabolism. Oxygenation of the aromatic ring is performed by a multisubunit phenylacetyl-coenzyme A oxygenase complex that shares remote homology of two subunits to well-studied bacterial multicomponent mono-oxygenases (BMMs) and was postulated to form a new BMM subfamily. We expressed the subunits PaaA,B,C,D,E of the PA-CoA oxygenase and showed that PaaABC, PaaAC and PaaBC form stable sub-complexes that can be purified. In vitro reconstitution of the oxygenase subunits showed that each of the PaaA,B,C and E subunits are necessary for catalysis, while PaaD is not essential. We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives. We conclude that PaaAC forms a catalytic core with a monooxygenase fold with PaaA being the catalytic alpha subunit and PaaC - the structural beta subunit. PaaAC forms hetero-tetramers that are organized very differently from other known multisubunit monooxygenases and lacks their conservative network of hydrogen bonds between the di-iron center and protein surface, suggesting different association with the reductase and different mechanism of electron transport. The PaaA structure shows adaptation of the common access route to the active site for binding a CoA-bound substrate. The enzyme-substrate complex shows the orientation of the aromatic ring, which is poised for oxygenation at the ortho-position, in accordance with the expected chemistry. The PA-CoA oxygenase complex serves as a paradigm for the new subfamily multicomponent monooxygenases comprising several hundreds of homologs.
Structural and functional studies of the Escherichia coli phenylacetyl-coa monooxygenase complex.,Grishin AM, Ajamian E, Tao L, Zhang L, Menard R, Cygler M J Biol Chem. 2011 Jan 19. PMID:21247899[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem. 1998 Oct 2;273(40):25974-86. PMID:9748275
- ↑ Fernandez C, Ferrandez A, Minambres B, Diaz E, Garcia JL. Genetic characterization of the phenylacetyl-coenzyme A oxygenase from the aerobic phenylacetic acid degradation pathway of Escherichia coli. Appl Environ Microbiol. 2006 Nov;72(11):7422-6. Epub 2006 Sep 22. PMID:16997993 doi:10.1128/AEM.01550-06
- ↑ Teufel R, Mascaraque V, Ismail W, Voss M, Perera J, Eisenreich W, Haehnel W, Fuchs G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14390-5. doi:, 10.1073/pnas.1005399107. Epub 2010 Jul 21. PMID:20660314 doi:10.1073/pnas.1005399107
- ↑ Grishin AM, Ajamian E, Tao L, Zhang L, Menard R, Cygler M. Structural and functional studies of the Escherichia coli phenylacetyl-coa monooxygenase complex. J Biol Chem. 2011 Jan 19. PMID:21247899 doi:10.1074/jbc.M110.194423
- ↑ Grishin AM, Ajamian E, Tao L, Zhang L, Menard R, Cygler M. Structural and functional studies of the Escherichia coli phenylacetyl-coa monooxygenase complex. J Biol Chem. 2011 Jan 19. PMID:21247899 doi:10.1074/jbc.M110.194423
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