1smv

From Proteopedia

(Difference between revisions)

Revision as of 07:30, 14 March 2018

PRIMARY STRUCTURE OF SESBANIA MOSAIC VIRUS COAT PROTEIN: ITS IMPLICATIONS TO THE ASSEMBLY AND ARCHITECTURE OF THE VIRUS

Structural highlights

1smv is a 3 chain structure with sequence from Sesbania mosaic virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: Sobemoviruses are a group of RNA plant viruses that have a narrow host range. They are characterized in vitro by their stability, high thermal inactivation point and longevity. The three-dimensional structure of only one virus belonging to this group, southern bean mosaic virus (SBMV), is known. Structural studies on sesbania mosaic virus (SMV), which is closely related to SBMV, will provide details of the molecular interactions that are likely to be important in the stability and assembly of sobemoviruses. RESULTS: We have determined the three-dimensional structure of SMV at 3 A resolution. The polypeptide fold and quaternary organization are very similar to those of SBMV. The capsid consists of sixty icosahedral asymmetric units, each comprising three copies of a chemically identical coat protein subunit, which are designated as A, B and C and are in structurally different environments. Four cation-binding sites have been located in the icosahedral asymmetric unit. Of these, the site at the quasi-threefold axis is not found in SBMV. Structural differences are observed in loops and regions close to this cation-binding site. Preliminary studies on ethylene diamine tetra acetic acid (EDTA) treated crystals suggest asymmetry in removal of the quasi-equivalent cations at the AB, BC, and AC subunit interfaces. CONCLUSIONS: Despite the overall similarity between SMV and SBMV in the nature of the polypeptide fold, these viruses show a number of differences in intermolecular interactions. The polar interactions at the quasi-threefold axis are substantially less in SMV and positively charged residues on the RNA-facing side of the protein and in the N-terminal arm are not particularly well conserved. This suggests that protein-RNA interactions are likely to be different between the two viruses.

Structure of sesbania mosaic virus at 3 A resolution.,Bhuvaneshwari M, Subramanya HS, Gopinath K, Savithri HS, Nayudu MV, Murthy MR Structure. 1995 Oct 15;3(10):1021-30. PMID:8589997^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bhuvaneshwari M, Subramanya HS, Gopinath K, Savithri HS, Nayudu MV, Murthy MR. Structure of sesbania mosaic virus at 3 A resolution. Structure. 1995 Oct 15;3(10):1021-30. PMID:8589997

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1smv"

Categories: Sesbania mosaic virus | Bhuvaneshwari, M | Murthy, M R.N | Icosahedral virus | Virus

@@ Line 1: / Line 1: @@
 ==PRIMARY STRUCTURE OF SESBANIA MOSAIC VIRUS COAT PROTEIN: ITS IMPLICATIONS TO THE ASSEMBLY AND ARCHITECTURE OF THE VIRUS==
 <StructureSection load='1smv' size='340' side='right' caption='[[1smv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1smv]] is a 3 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=1SMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SMV FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1smv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1smv OCA], [http://pdbe.org/1smv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1smv RCSB], [http://www.ebi.ac.uk/pdbsum/1smv PDBsum]</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=1smv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1smv OCA], [http://pdbe.org/1smv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1smv RCSB], [http://www.ebi.ac.uk/pdbsum/1smv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1smv ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 10: / Line 11: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sm/1smv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sm/1smv_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1smv

From Proteopedia

Revision as of 07:30, 14 March 2018

PRIMARY STRUCTURE OF SESBANIA MOSAIC VIRUS COAT PROTEIN: ITS IMPLICATIONS TO THE ASSEMBLY AND ARCHITECTURE OF THE VIRUS

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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Proteopedia Page Contributors and Editors (what is this?)

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