1td0

<table><tr><td colspan='2'>[[1td0]] is a 4 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=1TD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TD0 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=1td0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1td0 OCA], [https://pdbe.org/1td0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1td0 RCSB], [https://www.ebi.ac.uk/pdbsum/1td0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1td0 ProSAT]</span></td></tr>

[[https://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.

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== 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<ref>PMID:15504410</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1td0" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Enterobacteria phage p21]]

[[Category: Chang, C]]

[[Category: Forrer, P]]

[[Category: Ott, D]]

[[Category: Plueckthun, A]]

[[Category: Wlodawer, A]]

[[Category: Viral protein]]