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| | ==Crystal Structure of the PaaF-PaaG Hydratase-Isomerase Complex from E.coli== | | ==Crystal Structure of the PaaF-PaaG Hydratase-Isomerase Complex from E.coli== |
| - | <StructureSection load='4fzw' size='340' side='right' caption='[[4fzw]], [[Resolution|resolution]] 2.55Å' scene=''> | + | <StructureSection load='4fzw' size='340' side='right'caption='[[4fzw]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fzw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FZW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fzw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FZW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1393, JW1388, paaF, ydbR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), paaG, ydbT, b1394, JW1389 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4fzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzw OCA], [https://pdbe.org/4fzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fzw RCSB], [https://www.ebi.ac.uk/pdbsum/4fzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzw 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/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] </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=4fzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fzw OCA], [http://pdbe.org/4fzw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fzw RCSB], [http://www.ebi.ac.uk/pdbsum/4fzw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fzw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAAF_ECOLI PAAF_ECOLI]] Catalyzes the reversible conversion of enzymatically produced 2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA.<ref>PMID:20660314</ref> <ref>PMID:9748275</ref> [[http://www.uniprot.org/uniprot/PAAG_ECOLI PAAG_ECOLI]] Catalyzes the reversible conversion of the epoxide to 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA).<ref>PMID:12846838</ref> <ref>PMID:20660314</ref> <ref>PMID:9748275</ref> | + | [https://www.uniprot.org/uniprot/PAAG_ECOLI PAAG_ECOLI] Catalyzes the reversible conversion of the epoxide to 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA).<ref>PMID:12846838</ref> <ref>PMID:20660314</ref> <ref>PMID:9748275</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4fzw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4fzw" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Enoyl-CoA hydratase 3D structures|Enoyl-CoA hydratase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Enoyl-CoA hydratase]]
| + | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]] | + | [[Category: Cygler M]] |
| - | [[Category: Cygler, M]] | + | [[Category: Grishin AM]] |
| - | [[Category: Grishin, A M]] | + | |
| - | [[Category: Bsgi]]
| + | |
| - | [[Category: Crotonase fold]]
| + | |
| - | [[Category: Enzymes of the phenylacetate degradation pathway]]
| + | |
| - | [[Category: Isomerase-lyase complex]]
| + | |
| Structural highlights
Function
PAAG_ECOLI Catalyzes the reversible conversion of the epoxide to 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA).[1] [2] [3]
Publication Abstract from PubMed
Microbial anaerobic and so-called hybrid pathways for degradation of aromatic compounds contain beta-oxidation-like steps. These reactions convert the product of the opening of the aromatic ring to common metabolites. The hybrid phenylacetate degradation pathway is encoded in Escherichia coli by the paa operon containing genes for 10 enzymes. Previously, we have analyzed protein-protein interactions among the enzymes catalyzing the initial oxidation steps in the paa pathway (Grishin, A. M., Ajamian, E., Tao, L., Zhang, L., Menard, R., and Cygler, M. (2011) J. Biol. Chem. 286, 10735-10743). Here we report characterization of interactions between the remaining enzymes of this pathway and show another stable complex, PaaFG, an enoyl-CoA hydratase and enoyl-Coa isomerase, both belonging to the crotonase superfamily. These steps are biochemically similar to the well studied fatty acid beta-oxidation, which can be catalyzed by individual monofunctional enzymes, multifunctional enzymes comprising several domains, or enzymatic complexes such as the bacterial fatty acid beta-oxidation complex. We have determined the structure of the PaaFG complex and determined that although individually PaaF and PaaG are similar to enzymes from the fatty acid beta-oxidation pathway, the structure of the complex is dissimilar from bacterial fatty acid beta-oxidation complexes. The PaaFG complex has a four-layered structure composed of homotrimeric discs of PaaF and PaaG. The active sites of PaaF and PaaG are adapted to accept the intermediary components of the Paa pathway, different from those of the fatty acid beta-oxidation. The association of PaaF and PaaG into a stable complex might serve to speed up the steps of the pathway following the conversion of phenylacetyl-CoA to a toxic and unstable epoxide-CoA by PaaABCE monooxygenase.
Protein-protein interactions in the beta-oxidation part of the phenylacetate utilization pathway: crystal structure of the PaaF-PaaG hydratase-isomerase complex.,Grishin AM, Ajamian E, Zhang L, Rouiller I, Bostina M, Cygler M J Biol Chem. 2012 Nov 2;287(45):37986-96. doi: 10.1074/jbc.M112.388231. Epub 2012, Sep 7. PMID:22961985[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ismail W, El-Said Mohamed M, Wanner BL, Datsenko KA, Eisenreich W, Rohdich F, Bacher A, Fuchs G. Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli. Eur J Biochem. 2003 Jul;270(14):3047-54. PMID:12846838
- ↑ 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
- ↑ 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
- ↑ Grishin AM, Ajamian E, Zhang L, Rouiller I, Bostina M, Cygler M. Protein-protein interactions in the beta-oxidation part of the phenylacetate utilization pathway: crystal structure of the PaaF-PaaG hydratase-isomerase complex. J Biol Chem. 2012 Nov 2;287(45):37986-96. doi: 10.1074/jbc.M112.388231. Epub 2012, Sep 7. PMID:22961985 doi:http://dx.doi.org/10.1074/jbc.M112.388231
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