4qly

Crystal structure of CLA-ER, a novel enone reductase catalyzing a key step of a gut-bacterial fatty acid saturation metabolism, biohydrogenation

spinqualitylabelsall models 4qly, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qly is a 4 chain structure with sequence from Lactiplantibacillus plantarum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.005Å Ligands: FMN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function U6C5W9_LACPN Publication Abstract from PubMed Recently, a novel gut-bacterial fatty acid metabolism, saturation of polyunsaturated fatty acid, that modifies fatty acid composition of the host and expected to improve our health by altering lipid metabolism related to the onset of metabolic syndrome, was discovered in Lactobacillus plantarum AKU 1009a. Enzymes constituting the pathway catalyze sequential reactions of free fatty acids without CoA or acyl carrier protein (ACP). Among these enzymes, CLA-ER was identified as an enone reductase that can saturate the C=C bond in the 10-oxo-trans-11-octadecenoic acid (KetoB) to produce 10-oxo-octadecanoic acid (KetoC). This enzyme is the sole member of NADH oxidase/flavin reductase family that has been identified to exert an enone reduction activity. Here, we report both the structure of holo CLA-ER with cofactor FMN and KetoC-bound structure, which elucidate the structural basis of enone group recognition of free fatty acids and provide the unique catalytic mechanism as an enone reductase in NADH oxidase/flavin reductase family. A "cap" structure of CLA-ER underwent a large conformational change upon the KetoC binding. The resulting binding site adopts a sandglass shape and was positively charged at one side, which is suitable to recognize a fatty acid molecule with enone group. Based on the crystal structures and enzymatic activities of several mutants, we identified C51, F126 and Y101 as the critical residues for the reaction and proposed an alternative electron transfer pathway of CLA-ER. These findings expand our understanding on the complexity of fatty acid metabolism. This article is protected by copyright. All rights reserved. Structure and reaction mechanism of a novel enone reductase.,Hou F, Miyakawa T, Kitamura N, Takeuchi M, Park SB, Kishino S, Ogawa J, Tanokura M FEBS J. 2015 Feb 19. doi: 10.1111/febs.13239. PMID:25702712 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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