2UV8

Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 angstrom resolution

2UV8 の概要

• エントリーDOI: 10.2210/pdb2uv8/pdb
• 分子名称: FATTY ACID SYNTHASE SUBUNIT ALPHA (FAS2), FATTY ACID SYNTHASE SUBUNIT BETA (FAS1), FLAVIN MONONUCLEOTIDE (3 entities in total)
• 機能のキーワード: fatty acid biosynthesis, malonyl/palmitoyl transferase, phosphopantetheine, fatty acid synthase, transferase, oxidoreductase, lipid synthesis, substrate shuttling, acyl carrier protein, ketoacyl reductase, acetyl transferase, enoyl reductase, phosphorylation, ketoacyl synthase, fatty acid synthesis, multifunctional enzyme, nad, nadp, lyase, yeast, hydrolase, dehydratase
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 1310370.80

構造登録者

Leibundgut, M.,Jenni, S.,Frick, C.,Ban, N. (登録日: 2007-03-09, 公開日: 2007-04-17, 最終更新日: 2023-12-13)

主引用文献

Leibundgut, M.,Jenni, S.,Frick, C.,Ban, N.
Structural Basis for Substrate Delivery by Acyl Carrier Protein in the Yeast Fatty Acid Synthase
Science, 316:288-, 2007

PubMed Abstract: In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the Saccharomyces cerevisiae FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.

PubMed: 17431182
DOI: 10.1126/SCIENCE.1138249

実験手法

X-RAY DIFFRACTION (3.1 Å)