1EA3

Influenza virus M1 protein

Summary for 1EA3

• Entry DOI: 10.2210/pdb1ea3/pdb
• Related: 1AA7
• Descriptor: MATRIX PROTEIN M1 (2 entities in total)
• Functional Keywords: influenza virus, matrix protein
• Biological source: INFLUENZA A VIRUS
• Total number of polymer chains: 2
• Total formula weight: 36416.18

Authors

Arzt, S. (deposition date: 2000-11-03, release date: 2001-04-26, Last modification date: 2023-12-13)

Primary citation

Arzt, S.,Baudin, F.,Barge, A.,Timmins, P.,Burmeister, W.P.,Ruigrok, R.W.
Combined Results from Solution Studies on Intact Influenza Virus M1 Protein and from a New Crystal Form of its N-Terminal Domain Show that M1 is an Elongated Monomeric
Virology, 279:439-, 2001

PubMed Abstract: The amino-terminal domain of influenza A virus matrix protein (residues 1-164) was crystallized at pH 7 into a new crystal form in space group P1. This packing of the protein implies that M1(1-164) was monomeric in solution when it crystallized. Otherwise, the structure of the M1 fragment in the pH 7 crystals was the same as the monomers in crystals formed at pH 4 where crystal packing resulted in dimer formation [B. Sha and M. Luo, 1997, Nature Struct. Biol. 4, 239-244]. Analysis of intact M1 protein, the N-terminal domain, and the remaining C-terminal fragment (residues 165-252) in solution also showed that the N-terminal domain was monomeric with the same dimensions as determined from the crystal structure. Intact M1 protein was also monomeric but with an elongated shape due to the presence of the C-terminal part. Circular dichroism showed that the C-terminal part of M1 contained helical structure. A model for soluble M1 is presented, based on the assumption that the C-terminal domain is spherical, in which the N- and C-terminal domains are connected by a linker sequence which is available for proteolytic attack.

PubMed: 11162800
DOI: 10.1006/VIRO.2000.0727

Experimental method

X-RAY DIFFRACTION (2.3 Å)