7B3A

Crystal structure of PamZ

7B3A の概要

• エントリーDOI: 10.2210/pdb7b3a/pdb
• 分子名称: Putative Acyl-transferase domain protein, ACETYL COENZYME *A, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: gcn5-related n-acetyltransferase-like protein; paenilamicin; paenilamicin-gene cluster, transferase
• 由来する生物種: Paenibacillus larvae subsp. larvae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33175.90

構造登録者

Loll, B.,Dang, T.,Mainz, A.,Suessmuth, R.,Wahl, M.C. (登録日: 2020-11-30, 公開日: 2021-11-10, 最終更新日: 2024-01-31)

主引用文献

Dang, T.,Loll, B.,Muller, S.,Skobalj, R.,Ebeling, J.,Bulatov, T.,Gensel, S.,Gobel, J.,Wahl, M.C.,Genersch, E.,Mainz, A.,Sussmuth, R.D.
Molecular basis of antibiotic self-resistance in a bee larvae pathogen.
Nat Commun, 13:2349-2349, 2022

PubMed Abstract: Paenibacillus larvae, the causative agent of the devastating honey-bee disease American Foulbrood, produces the cationic polyketide-peptide hybrid paenilamicin that displays antibacterial and antifungal activity. Its biosynthetic gene cluster contains a gene coding for the N-acetyltransferase PamZ. We show that PamZ acts as self-resistance factor in Paenibacillus larvae by deactivation of paenilamicin. Using tandem mass spectrometry, nuclear magnetic resonance spectroscopy and synthetic diastereomers, we identified the N-terminal amino group of the agmatinamic acid as the N-acetylation site. These findings highlight the pharmacophore region of paenilamicin, which we very recently identified as a ribosome inhibitor. Here, we further determined the crystal structure of PamZ:acetyl-CoA complex at 1.34 Å resolution. An unusual tandem-domain architecture provides a well-defined substrate-binding groove decorated with negatively-charged residues to specifically attract the cationic paenilamicin. Our results will help to understand the mode of action of paenilamicin and its role in pathogenicity of Paenibacillus larvae to fight American Foulbrood.

PubMed: 35487884
DOI: 10.1038/s41467-022-29829-w

実験手法

X-RAY DIFFRACTION (1.34 Å)