2bsf: Difference between revisions
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New page: left|200px<br /> <applet load="2bsf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bsf, resolution 2.10Å" /> '''STRUCTURE OF THE C-... |
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== | ==Structure of the C-terminal receptor-binding domain of avian reovirus fibre sigmaC, Zn crystal form.== | ||
Avian reovirus fibre, a homo-trimer of the sigmaC protein, is responsible | <StructureSection load='2bsf' size='340' side='right'caption='[[2bsf]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bsf]] is a 1 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=2BSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BSF 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]] 2.1Å</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>, <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=2bsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsf OCA], [https://pdbe.org/2bsf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bsf RCSB], [https://www.ebi.ac.uk/pdbsum/2bsf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bsf 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/bs/2bsf_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=2bsf 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 responsible for primary host cell attachment. The protein expressed in bacteria forms elongated fibres comprised of a carboxy-terminal globular head domain and a slender shaft, and partial proteolysis yielded a carboxy-terminal protease-stable domain that was amenable to crystallisation. Here, we show that this fragment retains receptor-binding capability and report its structure, solved using two-wavelength anomalous diffraction and refined using data collected from three different crystal forms at 2.1 angstroms, 2.35 angstroms and 3.0 angstroms resolution. The carboxy-terminal globular domain has a beta-barrel fold with the same overall topology as the mammalian reovirus fibre (sigma1). However, the monomers of the sigmaC trimer show a more splayed-out arrangement than in the sigma1 structure. Also resolved are two triple beta-spiral repeats of the shaft or stalk domain. The presence in the sequence of heptad repeats amino-terminal to these triple beta-spiral repeats suggests that the unresolved portion of the shaft domain contains a triple alpha-helical coiled-coil structure. Implications for the function and stability of the sigmaC protein are discussed. | |||
Structure of the carboxy-terminal receptor-binding domain of avian reovirus fibre sigmaC.,Guardado Calvo P, Fox GC, Hermo Parrado XL, Llamas-Saiz AL, Costas C, Martinez-Costas J, Benavente J, van Raaij MJ J Mol Biol. 2005 Nov 18;354(1):137-49. Epub 2005 Sep 30. PMID:16236316<ref>PMID:16236316</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2bsf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Avian orthoreovirus]] | [[Category: Avian orthoreovirus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Fox GC]] | |||
[[Category: Fox | [[Category: Guardado Calvo P]] | ||
[[Category: | [[Category: Hermo Parrado XL]] | ||
[[Category: Parrado | [[Category: Llamas-Saiz AL]] | ||
[[Category: | [[Category: Van Raaij MJ]] | ||
[[Category: | |||
