6X5W

Peptide-bound structure of Marinomonas primoryensis peptide-binding domain

6X5W の概要

• エントリーDOI: 10.2210/pdb6x5w/pdb
• 分子名称: Antifreeze protein, peptide, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: peptide-binding domain, protein-binding domain, protein binding
• 由来する生物種: Marinomonas primoryensis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55232.35

構造登録者

Guo, S.,Davies, P.L. (登録日: 2020-05-27, 公開日: 2021-09-01, 最終更新日: 2026-01-21)

主引用文献

Guo, S.,Zahiri, H.,Stevens, C.,Spaanderman, D.C.,Milroy, L.G.,Ottmann, C.,Brunsveld, L.,Voets, I.K.,Davies, P.L.
Molecular basis for inhibition of adhesin-mediated bacterial-host interactions through a peptide-binding domain.
Cell Rep, 37:110002-110002, 2021

PubMed Abstract: Infections typically begin with pathogens adhering to host cells. For bacteria, this adhesion can occur through specific ligand-binding domains. We identify a 20-kDa peptide-binding domain (PBD) in a 1.5-MDa RTX adhesin of a Gram-negative marine bacterium that colonizes diatoms. The crystal structure of this Ca-dependent PBD suggests that it may bind the C termini of host cell-surface proteins. A systematic peptide library analysis reveals an optimal tripeptide sequence with 30-nM affinity for the PBD, and X-ray crystallography details its peptide-protein interactions. Binding of the PBD to the diatom partner of the bacteria can be inhibited or competed away by the peptide, providing a molecular basis for inhibiting bacterium-host interactions. We further show that this PBD is found in other bacteria, including human pathogens such as Vibrio cholerae and Aeromonas veronii. Here, we produce the PBD ortholog from A. veronii and demonstrate, using the same peptide inhibitor, how pathogens may be prevented from adhering to their hosts.

PubMed: 34788627
DOI: 10.1016/j.celrep.2021.110002

実験手法

X-RAY DIFFRACTION (1.8 Å)