View source for 1yc6


==Crystallographic Structure of the T=1 Particle of Brome Mosaic Virus==
<StructureSection load='1yc6' size='340' side='right'caption='[[1yc6]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yc6]] is a 30 chain structure with sequence from [https://en.wikipedia.org/wiki/Brome_mosaic_virus Brome mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YC6 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]] 2.9&#8491;</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=1yc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yc6 OCA], [https://pdbe.org/1yc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yc6 RCSB], [https://www.ebi.ac.uk/pdbsum/1yc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yc6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAPSD_BMV CAPSD_BMV] Capsid protein. Binds specifically to the subgenomic RNA4 to ensure selective packaging.
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== Publication Abstract from PubMed ==
T=1 icosahedral particles of amino terminally truncated brome mosaic virus (BMV) protein were created by treatment of the wild-type T=3 virus with 1M CaCl2 and crystallized from sodium malonate. Diffraction data were collected from frozen crystals to beyond 2.9 A resolution and the structure determined by molecular replacement and phase extension. The particles are composed of pentameric capsomeres from the wild-type virions which have reoriented with respect to the original particle pentameric axes by rotations of 37 degrees , and formed tenuous interactions with one another, principally through conformationally altered C-terminal polypeptides. Otherwise, the pentamers are virtually superimposable upon those of the original T=3 BMV particles. The T=1 particles, in the crystals, are not perfect icosahedra, but deviate slightly from exact symmetry, possibly due to packing interactions. This suggests that the T=1 particles are deformable, which is consistent with the loose arrangement of pentamers and latticework of holes that penetrate the surface. Atomic force microscopy showed that the T=3 to T=1 transition could occur by shedding of hexameric capsomeres and restructuring of remaining pentamers accompanied by direct condensation. Knowledge of the structures of the BMV wild-type and T=1 particles now permit us to propose a tentative model for that process. A comparison of the BMV T=1 particles was made with the reassembled T=1 particles produced from the coat protein of trypsin treated alfalfa mosaic virus (AlMV), another bromovirus. There is little resemblance between the two particles. The BMV particle, with a maximum diameter of 195 A, is made from distinctive pentameric capsomeres with large holes along the 3-fold axis, while the AlMV particle, of approximate maximum diameter 220 A, has subunits closely packed around the 3-fold axis, large holes along the 5-fold axis, and few contacts within pentamers. In both particles crucial linkages are made about icosahedral dyads.

Crystallographic structure of the T=1 particle of brome mosaic virus.,Larson SB, Lucas RW, McPherson A J Mol Biol. 2005 Feb 25;346(3):815-31. Epub 2005 Jan 12. PMID:15713465<ref>PMID:15713465</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brome mosaic virus]]
[[Category: Large Structures]]
[[Category: Larson SB]]
[[Category: Lucas RW]]
[[Category: McPherson A]]