3JSB
Crystal structure of the N-terminal domain of the Lymphocytic Choriomeningitis Virus L protein
Summary for 3JSB
Entry DOI | 10.2210/pdb3jsb/pdb |
Descriptor | RNA-directed RNA polymerase (2 entities in total) |
Functional Keywords | viral protein, vizier, structural genomics, marseilles structural genomics program @ afmb, msgp, nucleotide-binding, nucleotidyltransferase, rna replication, rna-directed rna polymerase, transferase, virion, rna binding protein |
Biological source | Lymphocytic choriomeningitis virus (LCMV) |
Cellular location | Virion: P14240 |
Total number of polymer chains | 2 |
Total formula weight | 47444.34 |
Authors | Morin, B.,Jamal, S.,Ferron, F.P.,Coutard, B.,Bricogne, G.,Canard, B.,Vonrhein, C.,Marseilles Structural Genomics Program @ AFMB (MSGP) (deposition date: 2009-09-10, release date: 2010-09-15, Last modification date: 2024-03-20) |
Primary citation | Morin, B.,Coutard, B.,Lelke, M.,Ferron, F.P.,Kerber, R.,Jamal, S.,Frangeul, A.,Baronti, C.,Charrel, R.,de Lamballerie, X.,Vonrhein, C.,Lescar, J.,Bricogne, G.,Gunther, S.,Canard, B. The N-terminal domain of the arenavirus L protein is an RNA endonuclease essential in mRNA transcription Plos Pathog., 6:e1001038-e1001038, 2010 Cited by PubMed Abstract: Arenaviridae synthesize viral mRNAs using short capped primers presumably acquired from cellular transcripts by a 'cap-snatching' mechanism. Here, we report the crystal structure and functional characterization of the N-terminal 196 residues (NL1) of the L protein from the prototypic arenavirus: lymphocytic choriomeningitis virus. The NL1 domain is able to bind and cleave RNA. The 2.13 Å resolution crystal structure of NL1 reveals a type II endonuclease α/β architecture similar to the N-terminal end of the influenza virus PA protein. Superimposition of both structures, mutagenesis and reverse genetics studies reveal a unique spatial arrangement of key active site residues related to the PD…(D/E)XK type II endonuclease signature sequence. We show that this endonuclease domain is conserved and active across the virus families Arenaviridae, Bunyaviridae and Orthomyxoviridae and propose that the arenavirus NL1 domain is the Arenaviridae cap-snatching endonuclease. PubMed: 20862324DOI: 10.1371/journal.ppat.1001038 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.13 Å) |
Structure validation
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