2vrs

From Proteopedia

(Difference between revisions)

Current revision

Structure of avian reovirus sigmaC117-326, C2 crystal form

Structural highlights

2vrs is a 3 chain structure with sequence from Avian orthoreovirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.75Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SIGC_ARVS1 Structural protein responsible for cell attachment. Induces cell apoptosis.^[1]

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

Avian reovirus fibre, a homo-trimer of the sigmaC protein, is a minor component of the avian reovirus outer capsid. It is anchored via a short N-terminal sequence to the inner capsid lambdaC pentamer, and its protruding globular C-terminal domain is responsible for primary host cell attachment. We have previously solved the structure of a receptor-binding fragment in which residues 160-191 form a triple beta-spiral and 196-326 a beta-barrel head domain. Here we have expressed, purified and crystallized a major sigmaC fragment comprising residues 117-326. Its structure, which was solved by molecular replacement using the previously determined receptor-binding domain structure and refined to 1.75 A (0.175 nm) resolution, reveals an alpha-helical triple coiled-coil connected to the previously solved structure by a zinc-ion-containing linker. The coiled-coil domain contains two chloride ion binding sites, as well as specific trimerization and registration sequences. The linker may act as a functionally important hinge.

Crystallographic structure of the alpha-helical triple coiled-coil domain of avian reovirus S1133 fibre.,Guardado-Calvo P, Fox GC, Llamas-Saiz AL, van Raaij MJ J Gen Virol. 2009 Mar;90(Pt 3):672-7. PMID:19218213^[2]

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

References

↑ Shih WL, Hsu HW, Liao MH, Lee LH, Liu HJ. Avian reovirus sigmaC protein induces apoptosis in cultured cells. Virology. 2004 Mar 30;321(1):65-74. PMID:15033566 doi:10.1016/j.virol.2003.12.004
↑ Guardado-Calvo P, Fox GC, Llamas-Saiz AL, van Raaij MJ. Crystallographic structure of the alpha-helical triple coiled-coil domain of avian reovirus S1133 fibre. J Gen Virol. 2009 Mar;90(Pt 3):672-7. PMID:19218213 doi:90/3/672

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vrs"

@@ Line 1: / Line 1: @@
 ==Structure of avian reovirus sigmaC117-326, C2 crystal form==
-<StructureSection load='2vrs' size='340' side='right' caption='[[2vrs]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+<StructureSection load='2vrs' size='340' side='right'caption='[[2vrs]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vrs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Avian_orthoreovirus Avian orthoreovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VRS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vrs]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Avian_orthoreovirus Avian orthoreovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.75&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bsf|2bsf]], [[2jjl|2jjl]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2vrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrs OCA], [http://pdbe.org/2vrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vrs RCSB], [http://www.ebi.ac.uk/pdbsum/2vrs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrs ProSAT]</span></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=2vrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrs OCA], [https://pdbe.org/2vrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vrs RCSB], [https://www.ebi.ac.uk/pdbsum/2vrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrs ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SIGC_ARVS1 SIGC_ARVS1] Structural protein responsible for cell attachment. Induces cell apoptosis.<ref>PMID:15033566</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 29: @@
 </div>
 <div class="pdbe-citations 2vrs" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>
@@ Line 32: / Line 37: @@
 </StructureSection>
 [[Category: Avian orthoreovirus]]
-[[Category: Benavente, J]]
+[[Category: Large Structures]]
-[[Category: Fox, G C]]
+[[Category: Benavente J]]
-[[Category: Guardado-Calvo, P]]
+[[Category: Fox GC]]
-[[Category: Llamas-Saiz, A L]]
+[[Category: Guardado-Calvo P]]
-[[Category: Raaij, M J.van]]
+[[Category: Llamas-Saiz AL]]
-[[Category: Alpha-helical coiled coil]]
+[[Category: Van Raaij MJ]]
-[[Category: Beta-barrel]]
-[[Category: Coiled coil]]
-[[Category: Receptor-binding]]
-[[Category: Triple beta-spiral]]
-[[Category: Viral protein]]
-[[Category: Virion]]

2vrs

From Proteopedia

Current revision

Structure of avian reovirus sigmaC117-326, C2 crystal form

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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