1td4
From Proteopedia
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|PDB= 1td4 |SIZE=350|CAPTION= <scene name='initialview01'>1td4</scene>, resolution 1.50Å | |PDB= 1td4 |SIZE=350|CAPTION= <scene name='initialview01'>1td4</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=DSN:D-SERINE'>DSN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1td3|1TD3]] | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1td4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1td4 RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TD4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1TD4 is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/15504410 15504410] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15504410 15504410] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage p21]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chang, C.]] | [[Category: Chang, C.]] | ||
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[[Category: shp]] | [[Category: shp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:54:27 2008'' |
Revision as of 20:54, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1TD3
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:54:27 2008
