7QAB

NMR Solution Structure of mussel adhesive protein Pvfp-5b

7QAB の概要

• エントリーDOI: 10.2210/pdb7qab/pdb
• NMR情報: BMRB: 51091
• 分子名称: PVFP-5 (1 entity in total)
• 機能のキーワード: adhesion proteins, bioadhesives, mussel foot proteins, coacervation, structural protein
• 由来する生物種: Perna viridis (Asian green mussel, Mytilus viridis)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9514.96

構造登録者

Morando, M.A.,Venturella, F.,Pastore, A.,Alfano, C. (登録日: 2021-11-16, 公開日: 2022-08-03, 最終更新日: 2024-10-09)

主引用文献

Morando, M.A.,Venturella, F.,Sollazzo, M.,Monaca, E.,Sabbatella, R.,Vetri, V.,Passantino, R.,Pastore, A.,Alfano, C.
Solution structure of recombinant Pvfp-5 beta reveals insights into mussel adhesion.
Commun Biol, 5:739-739, 2022

PubMed Abstract: Some marine organisms can resist to aqueous tidal environments and adhere tightly on wet surface. This behavior has raised increasing attention for potential applications in medicine, biomaterials, and tissue engineering. In mussels, adhesive forces to the rock are the resultant of proteinic fibrous formations called byssus. We present the solution structure of Pvfp-5β, one of the three byssal plaque proteins secreted by the Asian green mussel Perna viridis, and the component responsible for initiating interactions with the substrate. We demonstrate that Pvfp-5β has a stably folded structure in agreement with the presence in the sequence of two EGF motifs. The structure is highly rigid except for a few residues affected by slow local motions in the µs-ms time scale, and differs from the model calculated by artificial intelligence methods for the relative orientation of the EGF modules, which is something where computational methods still underperform. We also show that Pvfp-5β is able to coacervate even with no DOPA modification, giving thus insights both for understanding the adhesion mechanism of adhesive mussel proteins, and developing of biomaterials.

PubMed: 35879391
DOI: 10.1038/s42003-022-03699-w

実験手法

SOLUTION NMR