5I5O

Crystal Structure of N-terminal Domain of Matrix Protein of Thogoto Virus at Neutral pH.

Summary for 5I5O

• Entry DOI: 10.2210/pdb5i5o/pdb
• Related: 5I5N
• Descriptor: Matrix protein (2 entities in total)
• Functional Keywords: viral protein
• Biological source: Thogoto virus
• Total number of polymer chains: 2
• Total formula weight: 34431.45

Authors

Liu, Y.,Liang, H.,Yang, M. (deposition date: 2016-02-15, release date: 2016-08-17, Last modification date: 2024-11-20)

Primary citation

Yang, M.,Feng, F.,Liu, Y.,Wang, H.,Yang, Z.,Hou, W.,Liang, H.
pH-dependent conformational changes of a Thogoto virus matrix protein reveal mechanisms of viral assembly and uncoating
J.Gen.Virol., 97:2149-2156, 2016

PubMed 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.

PubMed: 27411929
DOI: 10.1099/jgv.0.000551

Experimental method

X-RAY DIFFRACTION (2.682 Å)