PDBsum entry 5i5o

Viral protein

PDB id: 5i5o

Contents

Protein chains

130 a.a.

Waters ×14

PDB id:

5i5o

Name:

Viral protein

Title:

Crystal structure of n-terminal domain of matrix protein of thogoto virus at neutral ph.

Structure:

Matrix protein. Chain: a, b. Fragment: unp residues 3-151. Engineered: yes

Source:

Thogoto virus. Organism_taxid: 11569. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.68Å R-factor: 0.273 R-free: 0.285

Authors:

Y.Liu,H.Liang,M.Yang

Key ref:

M.Yang et al. (2016). pH-dependent conformational changes of a Thogoto virus matrix protein reveal mechanisms of viral assembly and uncoating. J Gen Virol, 97, 2149-2156. PubMed id: 27411929 DOI: 10.1099/jgv.0.000551

Date:

15-Feb-16 Release date: 17-Aug-16

Protein chains

Q80A33  (ML_THOGV) -  Protein ML from Thogoto virus (isolate SiAr 126)

Seq: 304 a.a.

Struc: 130 a.a.

DOI no: 10.1099/jgv.0.000551

J Gen Virol 97:2149-2156 (2016)

PubMed id: 27411929

pH-dependent conformational changes of a Thogoto virus matrix protein reveal mechanisms of viral assembly and uncoating.

M.Yang, F.Feng, Y.Liu, H.Wang, Z.Yang, W.Hou, H.Liang.

ABSTRACT

Orthomyxoviruses are a family of ssRNA virus, including influenza virus, infectious salmon anaemia virus and Thogoto virus. The matrix proteins of orthomyxoviruses play crucial roles in some essential processes of the viral life cycle. However, the mechanisms of the matrix proteins involved in these processes remain incompletely understood. Currently, only the structure and function of the matrix protein from influenza virus have been studied. Here, we present the crystal structures of the N-terminal domain of matrix protein from Thogoto virus at pH 7.0 and 4.5. By analysing the structures, we identified the conformational changes of monomers and dimers in different pH conditions, mainly caused by two flexible loops, L3 and L5. These structural deviations would reflect the basis of viral capsid assembly or disassembly.