This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1td4

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:42, 14 March 2018

Crystal structure of VSHP_BPP21 in space group H3 with high resolution.

Structural highlights

1td4 is a 1 chain structure with sequence from Bpp21. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1td3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VSHP_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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1td4"

@@ Line 1: / Line 1: @@
 ==Crystal structure of VSHP_BPP21 in space group H3 with high resolution.==
 <StructureSection load='1td4' size='340' side='right' caption='[[1td4]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DSN:D-SERINE'>DSN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1td3|1td3]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1td4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1td4 OCA], [http://pdbe.org/1td4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1td4 RCSB], [http://www.ebi.ac.uk/pdbsum/1td4 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1td4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1td4 OCA], [http://pdbe.org/1td4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1td4 RCSB], [http://www.ebi.ac.uk/pdbsum/1td4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1td4 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/td/1td4_consurf.spt"</scriptWhenChecked>
+    <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/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1td4

From Proteopedia

Revision as of 07:42, 14 March 2018

Crystal structure of VSHP_BPP21 in space group H3 with high resolution.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox