1td4
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1td4.jpg|left|200px]] | [[Image:1td4.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1td4", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1td4| PDB=1td4 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal structure of VSHP_BPP21 in space group H3 with high resolution.''' | '''Crystal structure of VSHP_BPP21 in space group H3 with high resolution.''' | ||
| Line 30: | Line 27: | ||
[[Category: Plueckthun, A.]] | [[Category: Plueckthun, A.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
| - | [[Category: | + | [[Category: Shp]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:48:45 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:48, 3 May 2008
Crystal structure of VSHP_BPP21 in space group H3 with high resolution.
Overview
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.
About this Structure
1TD4 is a Single protein structure of sequence from Enterobacteria phage p21. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 09:48:45 2008
