1AA7

INFLUENZA VIRUS MATRIX PROTEIN CRYSTAL STRUCTURE AT PH 4.0

Summary for 1AA7

• Entry DOI: 10.2210/pdb1aa7/pdb
• Descriptor: INFLUENZA VIRUS MATRIX PROTEIN (2 entities in total)
• Functional Keywords: viral assembly, virion budding, transcription repressor, matrix protein
• Biological source: unidentified influenza virus
• Cellular location: Virion membrane ; Peripheral membrane protein ; Cytoplasmic side : P03485
• Total number of polymer chains: 2
• Total formula weight: 34804.40

Authors

Sha, B.,Luo, M. (deposition date: 1997-01-24, release date: 1998-01-28, Last modification date: 2024-02-07)

Primary citation

Sha, B.,Luo, M.
Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1.
Nat.Struct.Biol., 4:239-244, 1997

PubMed Abstract: Matrix protein (M1) of influenza virus is a bifunctional protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. It is therefore required that M1 binds both membrane and RNA simultaneously. The X-ray crystal structure of the N-terminal portion of type A influenza virus M1-amino acid residues 2-158-has been determined at 2.08 A resolution at pH 4.0. The protein forms a dimer. A highly positively charged region on the dimer surface is suitably positioned to bind RNA while the hydrophobic surface opposite the RNA binding region may be involved in interactions with the membrane. The membrane-binding hydrophobic surface could be buried or exposed after a conformational change.

PubMed: 9164466
DOI: 10.1038/nsb0397-239

Experimental method

X-RAY DIFFRACTION (2.08 Å)