The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1 - PubMed (original) (raw)
. 2001 Oct 10;289(1):34-44.
doi: 10.1006/viro.2001.1119.
Affiliations
- PMID: 11601915
- DOI: 10.1006/viro.2001.1119
Free article
The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1
A Harris et al. Virology. 2001.
Free article
Abstract
The influenza matrix protein (M1) forms a protein layer under the viral membrane and is essential for viral stability and integrity. M1 mediates the encapsidation of the viral RNPs into the viral membrane by its membrane and RNP-binding activities. In order to understand the roles of M1-M1 protein interactions in forming the M1 layer, X-ray crystallographic studies of a M1 fragment (1-162) were carried out at neutral pH and compared with an acidic pH structure. At neutral pH the asymmetric unit was a stacked dimer of M1. A long molecular ribbon of neutral stacked dimers was formed by translation as dictated by the P1 space group. The elongated ribbon had a positively charged stripe on one side of the ribbon. A similar M1-M1 stacking interface was also found in the acidic asymmetric unit. However, within the acidic stacked dimer the molecules were not straight, but rotated in relation to each other by slightly changing the M1-M1 stacking interface. The acidic structure possessed an additional M1-M1 twofold interface. Protein docking confirmed that the M1-M1 stacking and M1-M1 twofold interfaces could be used to form a double ribbon of M1 molecules. By iterative repetition of the rotated relationship among the M1 molecules, a helix of M1 was generated. These studies suggest that M1 has the ability to form straight or bent elongated ribbons and helices. These oligomers are consistent with previous electron microscopic studies of M1, which demonstrated that isolated M1 formed elongated and flexible ribbons when isolated from what appeared to be a helical shell of M1 in the influenza virus.
Copyright 2001 Academic Press.
Similar articles
- Zinc- and pH-dependent conformational transition in a putative interdomain linker region of the influenza virus matrix protein M1.
Okada A, Miura T, Takeuchi H. Okada A, et al. Biochemistry. 2003 Feb 25;42(7):1978-84. doi: 10.1021/bi027176t. Biochemistry. 2003. PMID: 12590584 - 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 monomer.
Arzt S, Baudin F, Barge A, Timmins P, Burmeister WP, Ruigrok RW. Arzt S, et al. Virology. 2001 Jan 20;279(2):439-46. doi: 10.1006/viro.2000.0727. Virology. 2001. PMID: 11162800 - Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export.
Huang X, Liu T, Muller J, Levandowski RA, Ye Z. Huang X, et al. Virology. 2001 Sep 1;287(2):405-16. doi: 10.1006/viro.2001.1067. Virology. 2001. PMID: 11531417 - Structural aspects of oligomerization taking place between the transmembrane alpha-helices of bitopic membrane proteins.
Arkin IT. Arkin IT. Biochim Biophys Acta. 2002 Oct 11;1565(2):347-63. doi: 10.1016/s0005-2736(02)00580-1. Biochim Biophys Acta. 2002. PMID: 12409206 Review. - Matrix proteins of enveloped viruses: a case study of Influenza A virus M1 protein.
Kordyukova LV, Shtykova EV, Baratova LA, Svergun DI, Batishchev OV. Kordyukova LV, et al. J Biomol Struct Dyn. 2019 Feb;37(3):671-690. doi: 10.1080/07391102.2018.1436089. Epub 2018 Feb 13. J Biomol Struct Dyn. 2019. PMID: 29388479 Review.
Cited by
- RNA to Rule Them All: Critical Steps in Lassa Virus Ribonucleoparticle Assembly and Recruitment.
Sänger L, Williams HM, Yu D, Vogel D, Kosinski J, Rosenthal M, Uetrecht C. Sänger L, et al. J Am Chem Soc. 2023 Dec 27;145(51):27958-27974. doi: 10.1021/jacs.3c07325. Epub 2023 Dec 17. J Am Chem Soc. 2023. PMID: 38104324 Free PMC article. - Peptide Models of the Cytoplasmic Tail of Influenza A/H1N1 Virus Hemagglutinin Expand Understanding its pH-Dependent Modes of Interaction with Matrix Protein M1.
Poboinev VV, Khrustalev VV, Akunevich AA, Shalygo NV, Stojarov AN, Khrustaleva TA, Kordyukova LV. Poboinev VV, et al. Protein J. 2023 Aug;42(4):288-304. doi: 10.1007/s10930-023-10101-z. Epub 2023 Mar 23. Protein J. 2023. PMID: 36952102 Free PMC article. - Phosphatidylinositol 4,5-Bisphosphate Mediates the Co-Distribution of Influenza A Hemagglutinin and Matrix Protein M1 at the Plasma Membrane.
Raut P, Obeng B, Waters H, Zimmerberg J, Gosse JA, Hess ST. Raut P, et al. Viruses. 2022 Nov 12;14(11):2509. doi: 10.3390/v14112509. Viruses. 2022. PMID: 36423118 Free PMC article. - A Review and Meta-Analysis of Influenza Interactome Studies.
Chua SCJH, Cui J, Engelberg D, Lim LHK. Chua SCJH, et al. Front Microbiol. 2022 Apr 21;13:869406. doi: 10.3389/fmicb.2022.869406. eCollection 2022. Front Microbiol. 2022. PMID: 35531276 Free PMC article. Review. - Protein Folding Interdiction Strategy for Therapeutic Drug Development in Viral Diseases: Ebola VP40 and Influenza A M1.
Bergasa-Caceres F, Rabitz HA. Bergasa-Caceres F, et al. Int J Mol Sci. 2022 Mar 31;23(7):3906. doi: 10.3390/ijms23073906. Int J Mol Sci. 2022. PMID: 35409264 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources