1td4
From Proteopedia
(New page: 200px<br /><applet load="1td4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1td4, resolution 1.50Å" /> '''Crystal structure of...) |
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| - | [[Image:1td4.jpg|left|200px]]<br /><applet load="1td4" size=" | + | [[Image:1td4.jpg|left|200px]]<br /><applet load="1td4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1td4, resolution 1.50Å" /> | caption="1td4, resolution 1.50Å" /> | ||
'''Crystal structure of VSHP_BPP21 in space group H3 with high resolution.'''<br /> | '''Crystal structure of VSHP_BPP21 in space group H3 with high resolution.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | SHP, the capsid-stabilizing protein of lambdoid phage 21, is highly | + | 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== | ==About this Structure== | ||
| - | 1TD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leuconostoc_phage_p37 Leuconostoc phage p37]. Full crystallographic information is available from [http:// | + | 1TD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leuconostoc_phage_p37 Leuconostoc phage p37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TD4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: shp]] | [[Category: shp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:22 2008'' |
Revision as of 13:12, 21 February 2008
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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 Leuconostoc phage p37. 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
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