4V59

Crystal structure of fatty acid synthase complexed with nadp+ from thermomyces lanuginosus at 3.1 angstrom resolution.

これはPDB形式変換不可エントリーです。

4V59 の概要

• エントリーDOI: 10.2210/pdb4v59/pdb
• 分子名称: FATTY ACID SYNTHASE ALPHA SUBUNITS, FATTY ACID SYNTHASE BETA SUBUNITS, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: fungal, dehydratase, enoyl reductase, ketoacyl synthase, ketoacyl reductase, malonyl/palmitoyl transferase, transferase, substrate shuttling, multifunctional enzyme, acyl carrier protein, fatty acid synthesis, acetyl transferase, fatty acid synthase
• 由来する生物種: THERMOMYCES LANUGINOSUS; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 2632545.46

構造登録者

Jenni, S.,Leibundgut, M.,Boehringer, D.,Frick, C.,Mikolasek, B.,Ban, N. (登録日: 2007-03-09, 公開日: 2014-07-09, 最終更新日: 2024-05-08)

主引用文献

Jenni, S.,Leibundgut, M.,Boehringer, D.,Frick, C.,Mikolasek, B.,Ban, N.
Structure of Fungal Fatty Acid Synthase and Implications for Iterative Substrate Shuttling
Science, 316:254-, 2007

PubMed Abstract: We report crystal structures of the 2.6-megadalton alpha6beta6 heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.

PubMed: 17431175
DOI: 10.1126/SCIENCE.1138248

実験手法

X-RAY DIFFRACTION (3.1 Å)