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2bac
From Proteopedia
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Crystal structure of CLA-producing fatty acid isomerase from P. acnes
Overview
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.
About this Structure
2BAC is a Single protein structure of sequence from Propionibacterium acnes with , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Jan 29 18:20:15 2008
