Structural highlights
Function
U5Y6P4_PERVI
Publication Abstract from PubMed
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-5beta, 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-5beta 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 micros-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-5beta 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.
Solution structure of recombinant Pvfp-5beta reveals insights into mussel adhesion.,Morando MA, Venturella F, Sollazzo M, Monaca E, Sabbatella R, Vetri V, Passantino R, Pastore A, Alfano C Commun Biol. 2022 Jul 25;5(1):739. doi: 10.1038/s42003-022-03699-w. PMID:35879391[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Morando MA, Venturella F, Sollazzo M, Monaca E, Sabbatella R, Vetri V, Passantino R, Pastore A, Alfano C. Solution structure of recombinant Pvfp-5beta reveals insights into mussel adhesion. Commun Biol. 2022 Jul 25;5(1):739. doi: 10.1038/s42003-022-03699-w. PMID:35879391 doi:https://dx.doi.org/10.1038/s42003-022-03699-w
