8DLE

Crosslinked Crystal Structure of the 8-amino-7-oxonanoate synthase, BioF, and Benzene Sulfonyl Fluoride-crypto Acyl Carrier Protein, BSF-ACP

8DLE の概要

• エントリーDOI: 10.2210/pdb8dle/pdb
• 分子名称: 8-amino-7-oxononanoate synthase, Acyl carrier protein, PYRIDOXAL-5'-PHOSPHATE, ... (7 entities in total)
• 機能のキーワード: biof, aons, crosslinking, acp, complex, plp, transferase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52574.77

構造登録者

Chen, A.,Davis, T.D.,Louie, G.V.,Bowman, M.E.,Noel, J.P.,Burkart, M.D. (登録日: 2022-07-07, 公開日: 2023-07-12, 最終更新日: 2024-07-24)

主引用文献

Chen, A.,Re, R.N.,Davis, T.D.,Tran, K.,Moriuchi, Y.W.,Wu, S.,La Clair, J.J.,Louie, G.V.,Bowman, M.E.,Clarke, D.J.,Mackay, C.L.,Campopiano, D.J.,Noel, J.P.,Burkart, M.D.
Visualizing the Interface of Biotin and Fatty Acid Biosynthesis through SuFEx Probes.
J.Am.Chem.Soc., 146:1388-1395, 2024

PubMed Abstract: Site-specific covalent conjugation offers a powerful tool to identify and understand protein-protein interactions. In this study, we discover that sulfur fluoride exchange (SuFEx) warheads effectively crosslink the acyl carrier protein (AcpP) with its partner BioF, a key pyridoxal 5'-phosphate (PLP)-dependent enzyme in the early steps of biotin biosynthesis by targeting a tyrosine residue proximal to the active site. We identify the site of crosslink by MS/MS analysis of the peptide originating from both partners. We further evaluate the BioF-AcpP interface through protein crystallography and mutational studies. Among the AcpP-interacting BioF surface residues, three critical arginine residues appear to be involved in AcpP recognition so that pimeloyl-AcpP can serve as the acyl donor for PLP-mediated catalysis. These findings validate an evolutionary gain-of-function for BioF, allowing the organism to build biotin directly from fatty acid biosynthesis through surface modifications selective for salt bridge formation with acidic AcpP residues.

PubMed: 38176024
DOI: 10.1021/jacs.3c10181

実験手法

X-RAY DIFFRACTION (2.3 Å)