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| - | [[Image:2o7a.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2o7a| PDB=2o7a | SCENE= }} | | {{STRUCTURE_2o7a| PDB=2o7a | SCENE= }} |
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| - | '''T4 lysozyme C-terminal fragment'''
| + | ===T4 lysozyme C-terminal fragment=== |
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| - | ==Overview==
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| - | Small proteins are generally observed to fold in an apparent two-state manner. Recently, however, more sensitive techniques have demonstrated that even seemingly single-domain proteins are actually made up of smaller subdomains. T4 lysozyme is one such protein. We explored the relative autonomy of its two individual subdomains and their contribution to the overall stability of T4 lysozyme by examining a circular permutation (CP13*) that relocates the N-terminal A-helix, creating subdomains that are contiguous in sequence. By determining the high-resolution structure of CP13* and characterizing its energy landscape using native state hydrogen exchange (NSHX), we show that connectivity between the subdomains is an important determinant of the energetic cooperativity but not structural integrity of the protein. The circular permutation results in a protein more easily able to populate a partially unfolded form in which the C-terminal subdomain is folded and the N-terminal subdomain is unfolded. We also created a fragment model of this intermediate and demonstrate using X-ray crystallography that its structure is identical to the corresponding residues in the full-length protein with the exception of a small network of hydrophobic interactions. In sum, we conclude that the C-terminal subdomain dominates the energetics of T4 lysozyme folding, and the A-helix serves an important role in coupling the two subdomains.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17400926}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17400926 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17400926}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Protein folding]] | | [[Category: Protein folding]] |
| | [[Category: Protein stability]] | | [[Category: Protein stability]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:24:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:41:08 2008'' |
Revision as of 10:41, 29 July 2008
Template:STRUCTURE 2o7a
T4 lysozyme C-terminal fragment
Template:ABSTRACT PUBMED 17400926
About this Structure
2O7A is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Exploring subdomain cooperativity in T4 lysozyme I: structural and energetic studies of a circular permutant and protein fragment., Cellitti J, Llinas M, Echols N, Shank EA, Gillespie B, Kwon E, Crowder SM, Dahlquist FW, Alber T, Marqusee S, Protein Sci. 2007 May;16(5):842-51. Epub 2007 Mar 30. PMID:17400926
Page seeded by OCA on Tue Jul 29 13:41:08 2008
