2L0Z

Solution structure of a zinc-binding domain from the Junin virus envelope glycoprotein

2L0Z の概要

• エントリーDOI: 10.2210/pdb2l0z/pdb
• 分子名称: glycoprotein G2, ZINC ION (2 entities in total)
• 機能のキーワード: zinc-binding domain, virus envelope glycoprotein, gpc, junin virus, arenavirus, viral protein
• 由来する生物種: Junin virus (JUNV)
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4870.41

構造登録者

Briknarova, K.,York, J.,Nunberg, J.H. (登録日: 2010-07-21, 公開日: 2010-11-10, 最終更新日: 2024-11-06)

主引用文献

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

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: 21068387
DOI: 10.1074/jbc.M110.166025

実験手法

SOLUTION NMR