PDBsum entry 4pus

Viral protein

PDB id: 4pus

Contents

Protein chains

158 a.a.

132 a.a.

Waters ×158

PDB id:

4pus

Name:

Viral protein

Title:

Crystal structure of influenza a virus matrix protein m1

Structure:

Matrix protein 1. Chain: a, b. Fragment: n-terminal domain (unp residues 2-165). Synonym: matrix protein m1. Engineered: yes

Source:

Influenza a virus. Organism_taxid: 381518. Strain: a/wilson-smith/1933 h1n1. Gene: m. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.20Å R-factor: 0.226 R-free: 0.264

Authors:

M.K.Safo,F.N.Musayev,P.D.Mosier,H.Xie,U.R.Desai

Key ref:

M.K.Safo et al. (2014). Crystal structures of influenza A virus matrix protein M1: variations on a theme. Plos One, 9, e109510. PubMed id: 25295515 DOI: 10.1371/journal.pone.0109510

Date:

13-Mar-14 Release date: 22-Oct-14

Protein chain

P05777  (M1_I33A0) -  Matrix protein 1 from Influenza A virus (strain A/Wilson-Smith/1933 H1N1)

Seq: 252 a.a.

Struc: 158 a.a.*

Protein chain

P05777  (M1_I33A0) -  Matrix protein 1 from Influenza A virus (strain A/Wilson-Smith/1933 H1N1)

Seq: 252 a.a.

Struc: 132 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1371/journal.pone.0109510

Plos One 9:e109510 (2014)

PubMed id: 25295515

Crystal structures of influenza A virus matrix protein M1: variations on a theme.

M.K.Safo, F.N.Musayev, P.D.Mosier, Q.Zhou, H.Xie, U.R.Desai.

ABSTRACT

Matrix protein 1 (M1) of the influenza A virus plays multiple roles in virion assembly and infection. Interest in the pH dependence of M1's multiple functions led us to study the effect of subtle pH changes on M1 structure, resulting in the elucidation of a unique low-pH crystal structure of the N1-165-domain of A/WSN/33 (H1N1) M1 that has never been reported. Although the 2.2 Å crystal structure of M1 N-terminus shows a dimer with the two monomers interacting in a face-to-face fashion at low pH as observed earlier, a 44° rotation of the second monomer has led to a significantly different dimer interface that possibly affects dimer stability. More importantly, while one of the monomers is fully defined, the N-terminal half of the second monomer shows considerable disorder that appears inherent in the protein and is potentially physiologically relevant. Such disorder has not been observed in any other previously reported structure at either low or high pH conditions, despite similar crystallization pH conditions. By comparing our novel N1-165-domain structure with other low-pH or neutral-pH M1 structures, it appears that M1 can energetically access different monomer and dimer conformations, as well as oligomeric states, with varying degree of similarities. The study reported here provides further insights into M1 oligomerization that may be essential for viral propagation and infectivity.