2vrs: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: '''Unreleased structure''' The entry 2vrs is ON HOLD until Paper Publication Authors: Guardado-Calvo, P., Fox, G.C., Llamas-Saiz, A.L., Benavente, J., van Raaij, M.J. Description: Stru...
 
OCA (talk | contribs)
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 2vrs is ON HOLD  until Paper Publication
==Structure of avian reovirus sigmaC117-326, C2 crystal form==
<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 [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='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='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'>[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vr/2vrs_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vrs ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


Authors: Guardado-Calvo, P., Fox, G.C., Llamas-Saiz, A.L., Benavente, J., van Raaij, M.J.
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<ref>PMID:19218213</ref>


Description: Structure of avian reovirus sigmaC117-326, C2 crystal form
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2vrs" style="background-color:#fffaf0;"></div>


 
==See Also==
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 08:55:06 2008''
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Avian orthoreovirus]]
[[Category: Large Structures]]
[[Category: Benavente J]]
[[Category: Fox GC]]
[[Category: Guardado-Calvo P]]
[[Category: Llamas-Saiz AL]]
[[Category: Van Raaij MJ]]

Latest revision as of 15:30, 13 December 2023

Structure of avian reovirus sigmaC117-326, C2 crystal form

2vrs, resolution 1.75Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA