4y4y: Difference between revisions

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'''Unreleased structure'''
==T=1 capsid structure of SeMV Ndel65CP fused with B-domain of S. aureus protein SpA at the N-terminus (C2 crystal form)==
<StructureSection load='4y4y' size='340' side='right' caption='[[4y4y]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4y4y]] is a 30 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y4Y FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vak|1vak]]</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=4y4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4y OCA], [http://pdbe.org/4y4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y4y RCSB], [http://www.ebi.ac.uk/pdbsum/4y4y PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The capsid protein (CP) of Sesbania mosaic virus (SeMV, a T=3 plant virus) consists of a disordered N-terminal R-domain and an ordered S-domain. Removal of the R-domain results in the formation of T=1 particles. In the current study, the R-domain was replaced with unrelated polypeptides of similar lengths: the B-domain of Staphylococcus aureus SpA, and SeMV encoded polypeptides P8 and P10. The chimeric proteins contained T=3 or larger virus-like particles (VLPs) and could not be crystallized. The presence of metal ions during purification resulted in a large number of heterogeneous nucleoprotein complexes. N65-B (R domain replaced with B domain) could also be purified in a dimeric form. Its crystal structure revealed T=1 particles devoid of metal ions and the B-domain was disordered. However, the B-domain was functional in N65-B VLPs, suggesting possible biotechnological applications. These studies illustrate the importance of N-terminal residues, metal ions and robustness of the assembly process.


The entry 4y4y is ON HOLD  until Paper Publication
Structural studies on chimeric Sesbania mosaic virus coat protein: Revisiting SeMV assembly.,Gulati A, Murthy A, Abraham A, Mohan K, Natraj U, Savithri HS, Murthy MR Virology. 2015 Dec 17;489:34-43. doi: 10.1016/j.virol.2015.11.029. PMID:26704627<ref>PMID:26704627</ref>


Authors: Gulati, A., Murthy, M.R.N.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: T=1 capsid structure of SeMV Ndel65CP fused with B-domain of S. aureus protein SpA at the N-terminus (C2 crystal form)
<div class="pdbe-citations 4y4y" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gulati, A]]
[[Category: Gulati, A]]
[[Category: Murthy, M.R.N]]
[[Category: Murthy, M R.N]]
[[Category: Chimeric vlp]]
[[Category: Coat protein]]
[[Category: In vitro assembly]]
[[Category: Virus]]
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