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| | <StructureSection load='4y4y' size='340' side='right'caption='[[4y4y]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='4y4y' size='340' side='right'caption='[[4y4y]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y4y]] is a 30 chain structure with sequence from [http://en.wikipedia.org/wiki/Sesbania_mosaic_virus Sesbania mosaic virus]. 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> | + | <table><tr><td colspan='2'>[[4y4y]] is a 30 chain structure with sequence from [https://en.wikipedia.org/wiki/Sesbania_mosaic_virus Sesbania mosaic virus] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vak|1vak]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spa, SAOUHSC_00069 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12558 Sesbania mosaic virus])</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=4y4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4y OCA], [https://pdbe.org/4y4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y4y RCSB], [https://www.ebi.ac.uk/pdbsum/4y4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y4y ProSAT]</span></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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y4y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SPA_STAA8 SPA_STAA8] [https://www.uniprot.org/uniprot/Q9EB06_9VIRU Q9EB06_9VIRU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Sesbania mosaic virus]] | | [[Category: Sesbania mosaic virus]] |
| - | [[Category: Gulati, A]] | + | [[Category: Staphylococcus aureus subsp. aureus NCTC 8325]] |
| - | [[Category: Murthy, M R.N]]
| + | [[Category: Gulati A]] |
| - | [[Category: Chimeric vlp]] | + | [[Category: Murthy MRN]] |
| - | [[Category: Coat protein]] | + | |
| - | [[Category: In vitro assembly]]
| + | |
| - | [[Category: Virus]]
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| Structural highlights
Function
SPA_STAA8 Q9EB06_9VIRU
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gulati A, Murthy A, Abraham A, Mohan K, Natraj U, Savithri HS, Murthy MR. Structural studies on chimeric Sesbania mosaic virus coat protein: Revisiting SeMV assembly. Virology. 2015 Dec 17;489:34-43. doi: 10.1016/j.virol.2015.11.029. PMID:26704627 doi:http://dx.doi.org/10.1016/j.virol.2015.11.029
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