2bsf: Difference between revisions
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== Structural highlights == | == 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> | <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=' | </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=' | <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> | <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> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Avian orthoreovirus]] | [[Category: Avian orthoreovirus]] | ||
[[Category: Large Structures]] | [[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: | |||
Latest revision as of 12:18, 9 May 2024
Structure of the C-terminal receptor-binding domain of avian reovirus fibre sigmaC, Zn crystal form.Structure of the C-terminal receptor-binding domain of avian reovirus fibre sigmaC, Zn crystal form.
Structural highlights
FunctionSIGC_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 PubMedAvian 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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