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| | <StructureSection load='1td3' size='340' side='right'caption='[[1td3]], [[Resolution|resolution]] 2.37Å' scene=''> | | <StructureSection load='1td3' size='340' side='right'caption='[[1td3]], [[Resolution|resolution]] 2.37Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1td3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp21 Bpp21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TD3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TD3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1td3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_P21 Enterobacteria phage P21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TD3 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1td4|1td4]]</div></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]] 2.37Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SHP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10711 BPP21])</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=1td3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1td3 OCA], [https://pdbe.org/1td3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1td3 RCSB], [https://www.ebi.ac.uk/pdbsum/1td3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1td3 ProSAT]</span></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=1td3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1td3 OCA], [http://pdbe.org/1td3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1td3 RCSB], [http://www.ebi.ac.uk/pdbsum/1td3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1td3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VSHP_BPP21 VSHP_BPP21]] Stabilizes the head shell following the rearrangement of the gp7 subunits of the head shell lattice that accompanies expansion of the head. | + | [https://www.uniprot.org/uniprot/DECO_BPP21 DECO_BPP21] Stabilizes the head shell following the rearrangement of the gp7 subunits of the head shell lattice that accompanies expansion of the head. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpp21]] | + | [[Category: Enterobacteria phage P21]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chang, C]] | + | [[Category: Chang C]] |
| - | [[Category: Forrer, P]] | + | [[Category: Forrer P]] |
| - | [[Category: Ott, D]] | + | [[Category: Ott D]] |
| - | [[Category: Plueckthun, A]] | + | [[Category: Plueckthun A]] |
| - | [[Category: Wlodawer, A]] | + | [[Category: Wlodawer A]] |
| - | [[Category: Shp]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
DECO_BPP21 Stabilizes the head shell following the rearrangement of the gp7 subunits of the head shell lattice that accompanies expansion of the head.
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
SHP, the capsid-stabilizing protein of lambdoid phage 21, is highly resistant against denaturant-induced unfolding. We demonstrate that this high functional stability of SHP is due to a high kinetic stability with a half-life for unfolding of 25 days at zero denaturant, while the thermodynamic stability is not unusually high. Unfolding experiments demonstrated that the trimeric state (also observed in crystals and present on the phage capsid) of SHP is kinetically stable in solution, while the monomer intermediate unfolds very rapidly. We also determined the crystal structure of trimeric SHP at 1.5A resolution, which was compared to that of its functional homolog gpD. This explains how a tight network of H-bonds rigidifies crucial interpenetrating residues, leading to the observed extremely slow trimer dissociation or denaturation. Taken as a whole, our results provide molecular-level insights into natural strategies to achieve kinetic stability by taking advantage of protein oligomerization. Kinetic stability may be especially needed in phage capsids to allow survival in harsh environments.
Kinetic stability and crystal structure of the viral capsid protein SHP.,Forrer P, Chang C, Ott D, Wlodawer A, Pluckthun A J Mol Biol. 2004 Nov 12;344(1):179-93. PMID:15504410[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Forrer P, Chang C, Ott D, Wlodawer A, Pluckthun A. Kinetic stability and crystal structure of the viral capsid protein SHP. J Mol Biol. 2004 Nov 12;344(1):179-93. PMID:15504410 doi:10.1016/j.jmb.2004.09.030
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