2b9y

Crystal structure of CLA-producing fatty acid isomerase from P. acnes

spinqualitylabelsall models 2b9y, resolution 2.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2b9y is a 1 chain structure with sequence from "bacillus_acnes"_gilchrist_1900 "bacillus acnes" gilchrist 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BU1, CL, FAD, SO4 Related: 2b9w, 2b9x, 2ba9, 2bab, 2bac Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Conjugated linoleic acids (CLAs) affect body fat gain, carcinogenesis, insulin resistance, and lipid peroxidation in mammals. Several isomers of CLA exist, of which the (9Z, 11E) and (10E, 12Z) isomers have beneficial effects on human metabolism but are scarce in foods. Bacterial polyunsaturated fatty acid isomerases are promising biotechnological catalysts for CLA production. We describe six crystal structures of the Propionibacterium acnes polyunsaturated fatty acid isomerase PAI in apo- and product-bound forms. The three-domain flavoprotein has previously undescribed folds outside the FAD-binding site. Conformational changes in a hydrophobic channel toward the active site reveal a unique gating mechanism for substrate specificity. The geometry of the substrate-binding site explains the length preferences for C18 fatty acids. A catalytic mechanism for double-bond isomerization is formulated that may be altered to change substrate specificity for syntheses of rare CLAs from easily accessible precursors. Structure and mechanism of the Propionibacterium acnes polyunsaturated fatty acid isomerase.,Liavonchanka A, Hornung E, Feussner I, Rudolph MG Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2576-81. Epub 2006 Feb 13. PMID:16477020 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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