2B9W

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

2B9W の概要

• エントリーDOI: 10.2210/pdb2b9w/pdb
• 関連するPDBエントリー: 2B9X 2B9Y 2BA9 2BAB 2BAC
• 分子名称: putative aminooxidase, SODIUM ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: isomerase, conjugated linoleic acid, fad
• 由来する生物種: Propionibacterium acnes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50556.15

構造登録者

Rudolph, M.G.,Liavonchanka, A. (登録日: 2005-10-13, 公開日: 2006-01-31, 最終更新日: 2024-03-13)

主引用文献

Liavonchanka, A.,Hornung, E.,Feussner, I.,Rudolph, M.G.
Structure and mechanism of the Propionibacterium acnes polyunsaturated fatty acid isomerase
Proc.Natl.Acad.Sci.Usa, 103:2576-2581, 2006

PubMed Abstract: 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.

PubMed: 16477020
DOI: 10.1073/pnas.0510144103

実験手法

X-RAY DIFFRACTION (1.95 Å)