5i72

Crystal structure of the oligomeric form of the Lassa virus matrix protein Z

spinqualitylabelsall models 5i72, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i72 is a 2 chain structure with sequence from Lassa virus Josiah. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Z_LASSJ Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L (By similarity). Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. Publication Abstract from PubMed 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. IMPORTANCE: The arenavirus Lassa causes hundreds of thousands of infections each year, many of which develop into fatal hemorrhagic fever. The arenavirus matrix protein Z is highly multifunctional, having at least four distinct roles in the virus life cycle. 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 Z and demonstrate that Z forms a "wreath" with a highly basic center. This structure, combined with 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. Crystal structure of the oligomeric form of the Lassa virus matrix protein Z.,Hastie KM, Zandonatti M, Liu T, Li S, Woods VL Jr, Saphire EO J Virol. 2016 Feb 24. pii: JVI.02896-15. PMID:26912609 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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