2VZ9

Crystal Structure of Mammalian Fatty Acid Synthase in complex with NADP

2VZ9 の概要

• エントリーDOI: 10.2210/pdb2vz9/pdb
• 関連するPDBエントリー: 2VZ8
• 分子名称: FATTY ACID SYNTHASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (2 entities in total)
• 機能のキーワード: transferase, phosphopantetheine, fatty acid synthase, multienzyme, megasynthase, fatty acid synthesis
• 由来する生物種: SUS SCROFA (PIG)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 548038.00

構造登録者

Maier, T.,Leibundgut, M.,Ban, N. (登録日: 2008-07-31, 公開日: 2008-09-09, 最終更新日: 2023-12-13)

主引用文献

Maier, T.,Leibundgut, M.,Ban, N.
The Crystal Structure of a Mammalian Fatty Acid Synthase.
Science, 321:1315-, 2008

PubMed Abstract: Mammalian fatty acid synthase is a large multienzyme that catalyzes all steps of fatty acid synthesis. We have determined its crystal structure at 3.2 angstrom resolution covering five catalytic domains, whereas the flexibly tethered terminal acyl carrier protein and thioesterase domains remain unresolved. The structure reveals a complex architecture of alternating linkers and enzymatic domains. Substrate shuttling is facilitated by flexible tethering of the acyl carrier protein domain and by the limited contact between the condensing and modifying portions of the multienzyme, which are mainly connected by linkers rather than direct interaction. The structure identifies two additional nonenzymatic domains: (i) a pseudo-ketoreductase and (ii) a peripheral pseudo-methyltransferase that is probably a remnant of an ancestral methyltransferase domain maintained in some related polyketide synthases. The structural comparison of mammalian fatty acid synthase with modular polyketide synthases shows how their segmental construction allows the variation of domain composition to achieve diverse product synthesis.

PubMed: 18772430
DOI: 10.1126/SCIENCE.1161269

実験手法

X-RAY DIFFRACTION (3.3 Å)