1f15: Difference between revisions

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 <StructureSection load='1f15' size='340' side='right'caption='[[1f15]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1f15]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucumber_mosaic_virus_(strain_fny) Cucumber mosaic virus (strain fny)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F15 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1f15]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucumber_mosaic_virus_(strain_FNY) Cucumber mosaic virus (strain FNY)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F15 FirstGlance]. <br>
-</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=1f15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f15 OCA], [https://pdbe.org/1f15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f15 RCSB], [https://www.ebi.ac.uk/pdbsum/1f15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f15 ProSAT]</span></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]] 3.2&#8491;</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=1f15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f15 OCA], [https://pdbe.org/1f15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f15 RCSB], [https://www.ebi.ac.uk/pdbsum/1f15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f15 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CAPSD_CMVFN CAPSD_CMVFN]] Capsid protein. Probably binds RNA and plays a role in packaging (By similarity).
+[https://www.uniprot.org/uniprot/CAPSD_CMVFN CAPSD_CMVFN] Capsid protein. Probably binds RNA and plays a role in packaging (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1f15 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The structure of cucumber mosaic virus (CMV; strain Fny) has been determined to a 3.2-A resolution using X-ray crystallography. Despite the fact that CMV has only 19% capsid protein sequence identity (34% similarity) to cowpea chlorotic mottle virus (CCMV), the core structures of these two members of the Bromoviridae family are highly homologous. As suggested by a previous low-resolution structural study, the 305-A diameter (maximum) of CMV is approximately 12 A larger than that of CCMV. In CCMV, the structures of the A, B, and C subunits are nearly identical except in their N termini. In contrast, the structures of two loops in subunit A of CMV differ from those in B and C. These loops are 6 and 7 residues longer than the analogous regions in CCMV. Unlike that of CCMV, the capsid of CMV does not undergo swelling at pH 7.0 and is stable at pH 9.0. This may be partly due to the fact that the N termini of the B and C subunits form a unique bundle of six amphipathic helices oriented down into the virion core at the threefold axes. In addition, while CCMV has a cluster of aspartic acid residues at the quasi-threefold axis that are proposed to bind metal in a pH-dependent manner, this cluster is replaced by complementing acids and bases in CMV. Finally, this structure clearly demonstrates that the residues important for aphid transmission lie at the outermost portion of the betaH-betaI loop and yields details of the portions of the virus that are hypothesized to mediate binding to aphid mouthparts.
-The structure of cucumber mosaic virus and comparison to cowpea chlorotic mottle virus.,Smith TJ, Chase E, Schmidt T, Perry KL J Virol. 2000 Aug;74(16):7578-86. PMID:10906212<ref>PMID:10906212</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1f15" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Chase, E]]
+[[Category: Chase E]]
-[[Category: Perry, K]]
+[[Category: Perry K]]
-[[Category: Schmidt, T]]
+[[Category: Schmidt T]]
-[[Category: Smith, T J]]
+[[Category: Smith TJ]]
-[[Category: Beta barrel]]
-[[Category: Icosahedral virus]]
-[[Category: Virus]]