4fzw

Crystal Structure of the PaaF-PaaG Hydratase-Isomerase Complex from E.coli

spinqualitylabelsall models 4fzw, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fzw is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Gene: b1393, JW1388, paaF, ydbR (ECOLI), paaG, ydbT, b1394, JW1389 (ECOLI) Activity: Enoyl-CoA hydratase, with EC number 4.2.1.17 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PAAF_ECOLI] Catalyzes the reversible conversion of enzymatically produced 2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA. [PAAG_ECOLI] Catalyzes the reversible conversion of the epoxide to 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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