4ggp

Crystal Structure of Selenomethionine containing Trans-2-Enoyl-CoA Reductase from Treponema denticola

spinqualitylabelsall models 4ggp, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ggp is a 4 chain structure with sequence from Treponema denticola ATCC 35405. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FABV_TREDE Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of the carbon-carbon double bond of crotonyl-CoA to yield butyryl-CoA. In vitro it can also use hexenoyl-CoA and dodecenoyl-CoA as substrates (PubMed:22906002). Publication Abstract from PubMed The production of fatty acids is an important cellular pathway for both cellular function and the development of engineered pathways for the synthesis of advanced biofuels. Despite the conserved reaction chemistry of various fatty acid synthase systems, the individual isozymes that catalyze these steps are quite diverse in their structural and biochemical features and are important for controlling differences at the cellular level. One of the key steps in the fatty acid elongation cycle is the enoyl-ACP (CoA) reductase function that drives the equilibrium forward toward chain extension. In this work, we report the structural and biochemical characterization of the trans-enoyl-CoA reductase from Treponema denticola (tdTer), which has been utilized for the engineering of synthetic biofuel pathways with an order of magnitude increase in product titers compared to those of pathways constructed with other enoyl-CoA reductase components. The crystal structure of tdTer was determined to 2.00 A resolution and shows that the Ter enzymes are distinct from members of the FabI, FabK, and FabL families but are highly similar to members of the FabV family. Further biochemical studies show that tdTer uses an ordered bi-bi mechanism initiated by binding of the NADH redox cofactor, which is consistent with the behavior of other enoyl-ACP (CoA) reductases. Mutagenesis of the substrate binding loop, characterization of enzyme activity with respect to crotonyl-CoA, hexenoyl-CoA, and dodecenoyl-CoA substrates, and product inhibition by lauroyl-CoA suggest that this region is important for controlling chain length specificity, with the major portal playing a more important role for longer chain length substrates. Biochemical and Structural Characterization of the trans-Enoyl-CoA Reductase from Treponema denticola.,Bond-Watts BB, Weeks AM, Chang MC Biochemistry. 2012 Aug 20. PMID:22906002 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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