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2bt7
From Proteopedia
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| - | [[Image:2bt7.gif|left|200px]]<br /> | ||
| - | <applet load="2bt7" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2bt7, resolution 2.35Å" /> | ||
| - | '''STRUCTURE OF THE C-TERMINAL RECEPTOR-BINDING DOMAIN OF AVIAN REOVIRUS FIBRE SIGMAC, CD CRYSTAL FORM'''<br /> | ||
| - | == | + | ==Structure of the C-terminal receptor-binding domain of avian reovirus fibre sigmaC, Cd crystal form== |
| - | Avian reovirus fibre, a homo-trimer of the sigmaC protein, is responsible | + | <StructureSection load='2bt7' size='340' side='right'caption='[[2bt7]], [[Resolution|resolution]] 2.35Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2bt7]] 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=2BT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BT7 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]] 2.35Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2bt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bt7 OCA], [https://pdbe.org/2bt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bt7 RCSB], [https://www.ebi.ac.uk/pdbsum/2bt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bt7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O12287_9VIRU O12287_9VIRU] | ||
| + | == 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/bt/2bt7_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=2bt7 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> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2bt7" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Avian orthoreovirus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fox GC]] | ||
| + | [[Category: Guardado Calvo P]] | ||
| + | [[Category: Hermo Parrado XL]] | ||
| + | [[Category: Llamas-Saiz AL]] | ||
| + | [[Category: Van Raaij MJ]] | ||
Current revision
Structure of the C-terminal receptor-binding domain of avian reovirus fibre sigmaC, Cd crystal form
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