PDBsum entry 4zpy

Virus

PDB id: 4zpy

Contents

Protein chain

549 a.a.

PDB id:

4zpy

Name:

Virus

Title:

Structure of n170a mvm mutant empty capsid

Structure:

Vp1 protein. Chain: a. Synonym: capsid protein vp1, coat protein vp1. Engineered: yes

Source:

Murine minute virus strain mvm prototype. Organism_taxid: 648235. Gene: vp1. Expressed in: insect cell expression vector ptie1. Expression_system_taxid: 266783

Resolution:

3.80Å R-factor: 0.283 R-free: 0.289

Authors:

P.Guerra,J.Querol-Audi,C.Silva,M.G.Mateu,N.Verdaguer

Key ref:

P.Guerra et al. (2017). Structural basis for biologically relevant mechanical stiffening of a virus capsid by cavity-creating or spacefilling mutations. Sci Rep, 7, 4101. PubMed id: 28642465

Date:

08-May-15 Release date: 24-May-17

Protein chain

P03137  (CAPSD_MUMIP) -  Capsid protein VP1 from Murine minute virus (strain MVM prototype)

Seq: 729 a.a.

Struc: 549 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Sci Rep 7:4101 (2017)

PubMed id: 28642465

Structural basis for biologically relevant mechanical stiffening of a virus capsid by cavity-creating or spacefilling mutations.

P.Guerra, A.Valbuena, J.Querol-Audí, C.Silva, M.Castellanos, A.Rodríguez-Huete, D.Garriga, M.G.Mateu, N.Verdaguer.

ABSTRACT

Recent studies reveal that the mechanical properties of virus particles may have been shaped by evolution to facilitate virus survival. Manipulation of the mechanical behavior of virus capsids is leading to a better understanding of viral infection, and to the development of virus-based nanoparticles with improved mechanical properties for nanotechnological applications. In the minute virus of mice (MVM), deleterious mutations around capsid pores involved in infection-related translocation events invariably increased local mechanical stiffness and interfered with pore-associated dynamics. To provide atomic-resolution insights into biologically relevant changes in virus capsid mechanics, we have determined by X-ray crystallography the structural effects of deleterious, mechanically stiffening mutations around the capsid pores. Data show that the cavity-creating N170A mutation at the pore wall does not induce any dramatic structural change around the pores, but instead generates subtle rearrangements that propagate throughout the capsid, resulting in a more compact, less flexible structure. Analysis of the spacefilling L172W mutation revealed the same relationship between increased stiffness and compacted capsid structure. Implications for understanding connections between virus mechanics, structure, dynamics and infectivity, and for engineering modified virus-based nanoparticles, are discussed.