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| | <StructureSection load='1yue' size='340' side='right'caption='[[1yue]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='1yue' size='340' side='right'caption='[[1yue]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yue]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YUE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yue]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YUE FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">24 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1yue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yue OCA], [http://pdbe.org/1yue PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yue RCSB], [http://www.ebi.ac.uk/pdbsum/1yue PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yue 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=1yue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yue OCA], [https://pdbe.org/1yue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yue RCSB], [https://www.ebi.ac.uk/pdbsum/1yue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yue ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAPSP_BPT4 CAPSP_BPT4]] Capsid protein that self-associates to form 11 pentons, building the T=13 laevo capsid in association with 160 hexamers of gp23* and one dodecamer of gp20.<ref>PMID:11162794</ref> <ref>PMID:15071181</ref> | + | [https://www.uniprot.org/uniprot/CAPSP_BPT4 CAPSP_BPT4] Capsid protein that self-associates to form 11 pentons, building the T=13 laevo capsid in association with 160 hexamers of gp23* and one dodecamer of gp20.<ref>PMID:11162794</ref> <ref>PMID:15071181</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1yue" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1yue" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[Retractions and Fraud|Retractions and Fraud]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpt4]] | + | [[Category: Escherichia virus T4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ahvazi, B]] | + | [[Category: Ahvazi B]] |
| - | [[Category: Black, L W]] | + | [[Category: Black LW]] |
| - | [[Category: Boeshans, K M]] | + | [[Category: Boeshans KM]] |
| - | [[Category: Fokine, A]] | + | [[Category: Fokine A]] |
| - | [[Category: Leiman, P G]] | + | [[Category: Leiman PG]] |
| - | [[Category: Mesyanzhinov, V V]] | + | [[Category: Mesyanzhinov VV]] |
| - | [[Category: Rossmann, M G]] | + | [[Category: Rossmann MG]] |
| - | [[Category: Shneider, M M]] | + | [[Category: Shneider MM]] |
| - | [[Category: Steven, A C]] | + | [[Category: Steven AC]] |
| - | [[Category: Bacteriophage]]
| + | |
| - | [[Category: Bacteriophage t4]]
| + | |
| - | [[Category: Capsid protein]]
| + | |
| - | [[Category: Gp24]]
| + | |
| - | [[Category: Hk97]]
| + | |
| - | [[Category: Mad]]
| + | |
| - | [[Category: Vertex]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
Function
CAPSP_BPT4 Capsid protein that self-associates to form 11 pentons, building the T=13 laevo capsid in association with 160 hexamers of gp23* and one dodecamer of gp20.[1] [2]
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 PubMed
Gene product (gp) 24 of bacteriophage T4 forms the pentameric vertices of the capsid. Using x-ray crystallography, we found the principal domain of gp24 to have a polypeptide fold similar to that of the HK97 phage capsid protein plus an additional insertion domain. Fitting gp24 monomers into a cryo-EM density map of the mature T4 capsid suggests that the insertion domain interacts with a neighboring subunit, effecting a stabilization analogous to the covalent crosslinking in the HK97 capsid. Sequence alignment and genetic data show that the folds of gp24 and the hexamer-forming capsid protein, gp23*, are similar. Accordingly, models of gp24* pentamers, gp23* hexamers, and the whole capsid were built, based on a cryo-EM image reconstruction of the capsid. Mutations in gene 23 that affect capsid shape map to the capsomer's periphery, whereas mutations that allow gp23 to substitute for gp24 at the vertices modify the interactions between monomers within capsomers. Structural data show that capsid proteins of most tailed phages, and some eukaryotic viruses, may have evolved from a common ancestor.
Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry.,Fokine A, Leiman PG, Shneider MM, Ahvazi B, Boeshans KM, Steven AC, Black LW, Mesyanzhinov VV, Rossmann MG Proc Natl Acad Sci U S A. 2005 May 17;102(20):7163-8. Epub 2005 May 6. PMID:15878991[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Olson NH, Gingery M, Eiserling FA, Baker TS. The structure of isometric capsids of bacteriophage T4. Virology. 2001 Jan 20;279(2):385-91. PMID:11162794 doi:http://dx.doi.org/10.1006/viro.2000.0735
- ↑ Fokine A, Chipman PR, Leiman PG, Mesyanzhinov VV, Rao VB, Rossmann MG. Molecular architecture of the prolate head of bacteriophage T4. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6003-8. Epub 2004 Apr 7. PMID:15071181 doi:http://dx.doi.org/10.1073/pnas.0400444101
- ↑ Fokine A, Leiman PG, Shneider MM, Ahvazi B, Boeshans KM, Steven AC, Black LW, Mesyanzhinov VV, Rossmann MG. Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry. Proc Natl Acad Sci U S A. 2005 May 17;102(20):7163-8. Epub 2005 May 6. PMID:15878991
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