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4V8L

Cryo-EM Structure of the Mycobacterial Fatty Acid Synthase

これはPDB形式変換不可エントリーです。
4V8L の概要
エントリーDOI10.2210/pdb4v8l/pdb
EMDBエントリー2238
分子名称FATTY ACID SYNTHASE, FLAVIN MONONUCLEOTIDE (2 entities in total)
機能のキーワードtransferase, mycolic acid biosynthesis, multifunctional enzyme, substrate channeling
由来する生物種MYCOBACTERIUM SMEGMATIS
タンパク質・核酸の鎖数6
化学式量合計1957287.56
構造登録者
Boehringer, D.,Ban, N.,Leibundgut, M. (登録日: 2012-12-06, 公開日: 2014-07-09, 最終更新日: 2024-05-08)
主引用文献Boehringer, D.,Ban, N.,Leibundgut, M.
7.5-A Cryo-Em Structure of the Mycobacterial Fatty Acid Synthase.
J.Mol.Biol., 425:841-, 2013
Cited by
PubMed Abstract: The mycobacterial fatty acid synthase (FAS) complex is a giant 2.0-MDa α(6) homohexameric multifunctional enzyme that catalyzes synthesis of fatty acid precursors of mycolic acids, which are major components of the cell wall in Mycobacteria and play an important role in pathogenicity. Here, we present a three-dimensional reconstruction of the Mycobacterium smegmatis FAS complex at 7.5Å, highly homologous to the Mycobacterium tuberculosis multienzyme, by cryo-electron microscopy. Based on the obtained structural data, which allowed us to identify secondary-structure elements, and sequence homology with the fungal FAS, we generated an accurate architectural model of the complex. The FAS system from Mycobacteria resembles a minimized version of the fungal FAS with much larger openings in the reaction chambers. These architectural features of the mycobacterial FAS may be important for the interaction with mycolic acid processing and condensing enzymes that further modify the precursors produced by FAS and for autoactivation of the FAS complex.
PubMed: 23291528
DOI: 10.1016/J.JMB.2012.12.021
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (7.5 Å)
構造検証レポート
Validation report summary of 4v8l
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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