7WX5

a Legionella acetyltransferase effector VipF

「7C4E」から置き換えられました

7WX5 の概要

• エントリーDOI: 10.2210/pdb7wx5/pdb
• 分子名称: N-acetyltransferase, ACETYL COENZYME *A (3 entities in total)
• 機能のキーワード: toxin, acetyltransferase, transferase
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36776.44

構造登録者

Chen, T.T.,Lin, Y.L.,Zhang, S.J.,Han, A.D. (登録日: 2022-02-14, 公開日: 2023-02-22, 最終更新日: 2024-04-03)

主引用文献

Chen, T.T.,Lin, Y.,Zhang, S.,Han, A.
Structural basis for the acetylation mechanism of the Legionella effector VipF.
Acta Crystallogr D Struct Biol, 78:1110-1119, 2022

PubMed Abstract: The pathogen Legionella pneumophila, which is the causative agent of Legionnaires' disease, secrets hundreds of effectors into host cells via its Dot/Icm secretion system to subvert host-cell pathways during pathogenesis. VipF, a conserved core effector among Legionella species, is a putative acetyltransferase, but its structure and catalytic mechanism remain unknown. Here, three crystal structures of VipF in complex with its cofactor acetyl-CoA and/or a substrate are reported. The two GNAT-like domains of VipF are connected as two wings by two β-strands to form a U-shape. Both domains bind acetyl-CoA or CoA, but only in the C-terminal domain does the molecule extend to the bottom of the U-shaped groove as required for an active transferase reaction; the molecule in the N-terminal domain folds back on itself. Interestingly, when chloramphenicol, a putative substrate, binds in the pocket of the central U-shaped groove adjacent to the N-terminal domain, VipF remains in an open conformation. Moreover, mutations in the central U-shaped groove, including Glu129 and Asp251, largely impaired the acetyltransferase activity of VipF, suggesting a unique enzymatic mechanism for the Legionella effector VipF.

PubMed: 36048151
DOI: 10.1107/S2059798322007318

実験手法

X-RAY DIFFRACTION (2.392 Å)