2l0z

From Proteopedia

(Difference between revisions)

Revision as of 07:37, 2 February 2022

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

Structural highlights

2l0z is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLYC_JUNIN] Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity). Glycoprotein G1 mediates virus attachment to host TFRC. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.^[1] Glycoprotein G2 is a class I viral fusion protein, that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversable conformational changes induced upon acidification in the endosome (By similarity).

Publication Abstract from PubMed

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 Junin 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.

Structure of a Zinc-binding Domain in the Junin Virus Envelope Glycoprotein.,Briknarova K, Thomas CJ, York J, Nunberg JH J Biol Chem. 2011 Jan 14;286(2):1528-36. Epub 2010 Nov 10. PMID:21068387^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Martinez MG, Forlenza MB, Candurra NA. Involvement of cellular proteins in Junin arenavirus entry. Biotechnol J. 2009 Jun;4(6):866-70. doi: 10.1002/biot.200800357. PMID:19548229 doi:http://dx.doi.org/10.1002/biot.200800357
↑ Briknarova K, Thomas CJ, York J, Nunberg JH. Structure of a Zinc-binding Domain in the Junin Virus Envelope Glycoprotein. J Biol Chem. 2011 Jan 14;286(2):1528-36. Epub 2010 Nov 10. PMID:21068387 doi:10.1074/jbc.M110.166025

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l0z"

@@ Line 3: / Line 3: @@
 <StructureSection load='2l0z' size='340' side='right'caption='[[2l0z]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l0z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2L0Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l0z]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L0Z FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2l0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0z OCA], [http://pdbe.org/2l0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l0z RCSB], [http://www.ebi.ac.uk/pdbsum/2l0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0z ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0z OCA], [https://pdbe.org/2l0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l0z RCSB], [https://www.ebi.ac.uk/pdbsum/2l0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0z ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GLYC_JUNIN GLYC_JUNIN]] Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity).  Glycoprotein G1 mediates virus attachment to host TFRC. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.<ref>PMID:19548229</ref>   Glycoprotein G2 is a class I viral fusion protein, that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversable conformational changes induced upon acidification in the endosome (By similarity).
+[[https://www.uniprot.org/uniprot/GLYC_JUNIN GLYC_JUNIN]] Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (By similarity).  Glycoprotein G1 mediates virus attachment to host TFRC. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.<ref>PMID:19548229</ref>   Glycoprotein G2 is a class I viral fusion protein, that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversable conformational changes induced upon acidification in the endosome (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2l0z

From Proteopedia

Revision as of 07:37, 2 February 2022

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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