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| | ==CRYSTAL STRUCTURE OF VACCINIA VIRUS A6 N-TERMINUS (SPACE GROUP C2)== | | ==CRYSTAL STRUCTURE OF VACCINIA VIRUS A6 N-TERMINUS (SPACE GROUP C2)== |
| - | <StructureSection load='6cb6' size='340' side='right' caption='[[6cb6]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='6cb6' size='340' side='right'caption='[[6cb6]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cb6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CB6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cb6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_Copenhagen Vaccinia virus Copenhagen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CB6 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x3w|4x3w]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cb6 OCA], [http://pdbe.org/6cb6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cb6 RCSB], [http://www.ebi.ac.uk/pdbsum/6cb6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cb6 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=6cb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cb6 OCA], [https://pdbe.org/6cb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cb6 RCSB], [https://www.ebi.ac.uk/pdbsum/6cb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cb6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A6_VACCC A6_VACCC]] Plays an essential role in immature virion (IV) to mature virion (MV) transition. | + | [https://www.uniprot.org/uniprot/PG132_VACCC PG132_VACCC] Lipid-bound viral membrane assembly protein that plays an essential role in immature virion (IV) to mature virion (MV) transition (PubMed:29915071). Functions in both crescent-shaped viral membranes formation and its enclosure to form immature virions. In addition, participates in targeting mature virion proteins to sites of virion assembly to ensure their proper localization.[UniProtKB:P29192]<ref>PMID:29915071</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Deng, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Han, Y]]
| + | [[Category: Vaccinia virus Copenhagen]] |
| - | [[Category: Zhang, B]]
| + | [[Category: Deng J]] |
| - | [[Category: A6]]
| + | [[Category: Han Y]] |
| - | [[Category: Poxviruse]]
| + | [[Category: Zhang B]] |
| - | [[Category: Vaccinia virus]] | + | |
| - | [[Category: Viral protein]] | + | |
| - | [[Category: Virion core protein]] | + | |
| - | [[Category: Virion morphogenesis]] | + | |
| Structural highlights
Function
PG132_VACCC Lipid-bound viral membrane assembly protein that plays an essential role in immature virion (IV) to mature virion (MV) transition (PubMed:29915071). Functions in both crescent-shaped viral membranes formation and its enclosure to form immature virions. In addition, participates in targeting mature virion proteins to sites of virion assembly to ensure their proper localization.[UniProtKB:P29192][1]
Publication Abstract from PubMed
Cellular membranes are maintained as closed compartments, broken up only transiently during membrane reorganization or lipid transportation. However, open-ended membranes, likely derived from scissions of the endoplasmic reticulum, persist in vaccinia virus-infected cells during the assembly of the viral envelope. A group of viral membrane assembly proteins (VMAPs) were identified as essential for this process. To understand the mechanism of VMAPs, we determined the 2.2-A crystal structure of the largest member, named A6, which is a soluble protein with two distinct domains. The structure of A6 displays a novel protein fold composed mainly of alpha helices. The larger C-terminal domain forms a unique cage that encloses multiple glycerophospholipids with a lipid bilayer-like configuration. The smaller N-terminal domain does not bind lipid but negatively affects lipid binding by A6. Mutations of key hydrophobic residues lining the lipid-binding cage disrupt lipid binding and abolish viral replication. Our results reveal a protein modality for enclosing the lipid bilayer and provide molecular insight into a viral machinery involved in generating and/or stabilizing open-ended membranes.
Structure of a lipid-bound viral membrane assembly protein reveals a modality for enclosing the lipid bilayer.,Pathak PK, Peng S, Meng X, Han Y, Zhang B, Zhang F, Xiang Y, Deng J Proc Natl Acad Sci U S A. 2018 Jun 18. pii: 1805855115. doi:, 10.1073/pnas.1805855115. PMID:29915071[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pathak PK, Peng S, Meng X, Han Y, Zhang B, Zhang F, Xiang Y, Deng J. Structure of a lipid-bound viral membrane assembly protein reveals a modality for enclosing the lipid bilayer. Proc Natl Acad Sci U S A. 2018 Jun 18. pii: 1805855115. doi:, 10.1073/pnas.1805855115. PMID:29915071 doi:http://dx.doi.org/10.1073/pnas.1805855115
- ↑ Pathak PK, Peng S, Meng X, Han Y, Zhang B, Zhang F, Xiang Y, Deng J. Structure of a lipid-bound viral membrane assembly protein reveals a modality for enclosing the lipid bilayer. Proc Natl Acad Sci U S A. 2018 Jun 18. pii: 1805855115. doi:, 10.1073/pnas.1805855115. PMID:29915071 doi:http://dx.doi.org/10.1073/pnas.1805855115
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