3KWV

Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers

3KWV の概要

• エントリーDOI: 10.2210/pdb3kwv/pdb
• 分子名称: Protective antigen PA-63, Lethal factor, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: bacillus anthracis, protective antigen, lethal factor, lethal toxin, octamer, protein transport, toxin, protein unfolding, protein translocation, cleavage on pair of basic residues, metal-binding, secreted, virulence, hydrolase, metalloprotease, protease, toxin-protein transport complex, toxin/protein transport
• 由来する生物種: Bacillus anthracis; 詳細
• 細胞内の位置: Secreted, extracellular space: P13423; Secreted: P15917
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 307350.72

構造登録者

Feld, G.K.,Kintzer, A.F.,Krantz, B.A. (登録日: 2009-12-01, 公開日: 2010-11-10, 最終更新日: 2023-09-06)

主引用文献

Feld, G.K.,Thoren, K.L.,Kintzer, A.F.,Sterling, H.J.,Tang, I.I.,Greenberg, S.G.,Williams, E.R.,Krantz, B.A.
Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers.
Nat.Struct.Mol.Biol., 17:1383-1390, 2010

PubMed Abstract: The protein transporter anthrax lethal toxin is composed of protective antigen (PA), a transmembrane translocase, and lethal factor (LF), a cytotoxic enzyme. After its assembly into holotoxin complexes, PA forms an oligomeric channel that unfolds LF and translocates it into the host cell. We report the crystal structure of the core of a lethal toxin complex to 3.1-Å resolution; the structure contains a PA octamer bound to four LF PA-binding domains (LF(N)). The first α-helix and β-strand of each LF(N) unfold and dock into a deep amphipathic cleft on the surface of the PA octamer, which we call the α clamp. The α clamp possesses nonspecific polypeptide binding activity and is functionally relevant to efficient holotoxin assembly, PA octamer formation, and LF unfolding and translocation. This structure provides insight into the mechanism of translocation-coupled protein unfolding.

PubMed: 21037566
DOI: 10.1038/nsmb.1923

実験手法

X-RAY DIFFRACTION (3.101 Å)