1td4
From Proteopedia
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| - | [[Image:1td4.jpg|left|200px]] | ||
| - | < | + | ==Crystal structure of VSHP_BPP21 in space group H3 with high resolution.== |
| - | + | <StructureSection load='1td4' size='340' side='right'caption='[[1td4]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1td4]] is a 1 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=1TD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TD4 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]] 1.5Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DSN:D-SERINE'>DSN</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=1td4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1td4 OCA], [https://pdbe.org/1td4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1td4 RCSB], [https://www.ebi.ac.uk/pdbsum/1td4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1td4 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [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 == | |
| - | == | + | [[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/td/1td4_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1td4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | 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<ref>PMID:15504410</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Enterobacteria phage | + | <div class="pdbe-citations 1td4" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Chang | + | <references/> |
| - | [[Category: Forrer | + | __TOC__ |
| - | [[Category: Ott | + | </StructureSection> |
| - | [[Category: Plueckthun | + | [[Category: Enterobacteria phage P21]] |
| - | [[Category: Wlodawer | + | [[Category: Large Structures]] |
| - | + | [[Category: Chang C]] | |
| - | + | [[Category: Forrer P]] | |
| + | [[Category: Ott D]] | ||
| + | [[Category: Plueckthun A]] | ||
| + | [[Category: Wlodawer A]] | ||
Current revision
Crystal structure of VSHP_BPP21 in space group H3 with high resolution.
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