2L0Z
Solution structure of a zinc-binding domain from the Junin virus envelope glycoprotein
Summary for 2L0Z
| Entry DOI | 10.2210/pdb2l0z/pdb |
| Descriptor | glycoprotein G2, ZINC ION (2 entities in total) |
| Functional Keywords | zinc-binding domain, virus envelope glycoprotein, gpc, junin virus, arenavirus, viral protein |
| Biological source | Junin virus (JUNV) |
| Cellular location | Stable signal peptide: Virion membrane; Multi-pass membrane protein (Potential). Glycoprotein G1: Virion membrane; Peripheral membrane protein (Potential). Glycoprotein G2: Virion membrane; Single- pass membrane protein (Potential): P26313 |
| Total number of polymer chains | 1 |
| Total formula weight | 4870.41 |
| Authors | Briknarova, K.,York, J.,Nunberg, J.H. (deposition date: 2010-07-21, release date: 2010-11-10, Last modification date: 2024-11-06) |
| Primary citation | Briknarova, K.,Thomas, C.J.,York, J.,Nunberg, J.H. Structure of a Zinc-binding Domain in the Junin Virus Envelope Glycoprotein. J.Biol.Chem., 286:1528-1536, 2011 Cited by PubMed Abstract: Arenaviruses cause acute hemorrhagic fevers with high mortality. Entry of the virus into the host cell is mediated by the viral envelope glycoprotein, GPC. In contrast to other class I viral envelope glycoproteins, the mature GPC complex contains a cleaved stable signal peptide (SSP) in addition to the canonical receptor-binding (G1) and transmembrane fusion (G2) subunits. SSP is critical for intracellular transport of the GPC complex to the cell surface and for its membrane-fusion activity. Previous studies have suggested that SSP is retained in GPC through interaction with a zinc-binding domain (ZBD) in the cytoplasmic tail of G2. Here we used NMR spectroscopy to determine the structure of Junín virus (JUNV) ZBD (G2 residues 445-485) and investigate its interaction with a conserved Cys residue (Cys-57) in SSP. We show that JUNV ZBD displays a novel fold containing two zinc ions. One zinc ion is coordinated by His-447, His-449, Cys-455, and His-485. The second zinc ion is coordinated by His-459, Cys-467, and Cys-469 and readily accepts Cys-57 from SSP as the fourth ligand. Our studies describe the structural basis for retention of the unique SSP subunit and suggest a mechanism whereby SSP is positioned in the GPC complex to modulate pH-dependent membrane fusion. PubMed: 21068387DOI: 10.1074/jbc.M110.166025 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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