title: Crystal Structure of the Oligomeric Form of Lassa Virus Matrix Protein Z.
abstract: The arenavirus matrix protein Z is highly multifunctional and occurs in both monomeric and oligomeric forms. The crystal structure of a dodecamer of Z from Lassa virus, presented here, illustrates a ring-like structure with a highly basic center. Mutagenesis demonstrates that the dimeric interface within the dodecamer and a Lys-Trp-Lys triad at the center of the ring are important for oligomerization. This structure provides an additional template to explore the many functions of Z.
  
  
  OBJECTIVE
  The arenavirus Lassa virus causes hundreds of thousands of infections each year, many of which develop into fatal hemorrhagic fever. The arenavirus matrix protein Z is multifunctional, with at least four distinct roles. Z exists in both monomeric and oligomeric forms, each of which likely serves a specific function in the viral life cycle. Here we present the dodecameric form of Lassa virus Z and demonstrate that Z forms a "wreath" with a highly basic center. This structure and that of monomeric Z now provide a pair of critical templates by which the multiple roles of Z in the viral life cycle may be interpreted.
authors.affiliation: Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.
authors.forename: Kathryn M
authors.initials: KM
authors.lastname: Hastie
authors.affiliation: Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.
authors.forename: Michelle
authors.initials: M
authors.lastname: Zandonatti
authors.affiliation: Department of Medicine, University of California-San Diego, La Jolla, California, USA.
authors.forename: Tong
authors.initials: T
authors.lastname: Liu
authors.affiliation: Department of Medicine, University of California-San Diego, La Jolla, California, USA.
authors.forename: Sheng
authors.initials: S
authors.lastname: Li
authors.affiliation: Department of Medicine, University of California-San Diego, La Jolla, California, USA.
authors.forename: Virgil L
authors.initials: VL
authors.lastname: Woods
authors.affiliation: Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA erica@scripps.edu.
authors.forename: Erica Ollmann
authors.initials: EO
authors.lastname: Saphire
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D007836:Lassa virus; D013058:Mass Spectrometry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D055503:Protein Multimerization; D016601:RNA-Binding Proteins; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D013329:Structure-Activity Relationship; D014763:Viral Matrix Proteins / Q000737:chemistry*
chemical_list: D002352:Carrier Proteins; D016601:RNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D014763:Viral Matrix Proteins; C487631:protein Z, Lassa virus