View source for 6cb7


==CRYSTAL STRUCTURE OF VACCINIA VIRUS A6 N-TERMINUS (SPACE GROUP C2)==
<StructureSection load='6cb7' size='340' side='right'caption='[[6cb7]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6cb7]] 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=6CB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CB7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=6cb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cb7 OCA], [https://pdbe.org/6cb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cb7 RCSB], [https://www.ebi.ac.uk/pdbsum/6cb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cb7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A6_VACCC A6_VACCC] Plays an essential role in immature virion (IV) to mature virion (MV) transition.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:29915071</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6cb7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vaccinia virus Copenhagen]]
[[Category: Deng J]]
[[Category: Han Y]]
[[Category: Zhang B]]