1rfo
From Proteopedia
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|LIGAND= | |LIGAND= | ||
|ACTIVITY= | |ACTIVITY= | ||
| - | |GENE= wac ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= wac ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rfo OCA], [http://www.ebi.ac.uk/pdbsum/1rfo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rfo RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1RFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFO OCA]. |
==Reference== | ==Reference== | ||
Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin., Guthe S, Kapinos L, Moglich A, Meier S, Grzesiek S, Kiefhaber T, J Mol Biol. 2004 Apr 2;337(4):905-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15033360 15033360] | Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin., Guthe S, Kapinos L, Moglich A, Meier S, Grzesiek S, Kiefhaber T, J Mol Biol. 2004 Apr 2;337(4):905-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15033360 15033360] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage t4]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Grzesiek, S.]] | [[Category: Grzesiek, S.]] | ||
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[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''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 23:27:29 2008'' |
Revision as of 20:27, 30 March 2008
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| Gene: | wac (Enterobacteria phage T4) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Trimeric Foldon of the T4 phagehead fibritin
Overview
The foldon domain constitutes the C-terminal 30 amino acid residues of the trimeric protein fibritin from bacteriophage T4. Its function is to promote folding and trimerization of fibritin. We investigated structure, stability and folding mechanism of the isolated foldon domain. The domain folds into the same trimeric beta-propeller structure as in fibritin and undergoes a two-state unfolding transition from folded trimer to unfolded monomers. The folding kinetics involve several consecutive reactions. Structure formation in the region of the single beta-hairpin of each monomer occurs on the submillisecond timescale. This reaction is followed by two consecutive association steps with rate constants of 1.9(+/-0.5)x10(6)M(-1)s(-1) and 5.4(+/-0.3)x10(6)M(-1)s(-1) at 0.58 M GdmCl, respectively. This is similar to the fastest reported bimolecular association reactions for folding of dimeric proteins. At low concentrations of protein, folding shows apparent third-order kinetics. At high concentrations of protein, the reaction becomes almost independent of protein concentrations with a half-time of about 3 ms, indicating that a first-order folding step from a partially folded trimer to the native protein (k=210 +/- 20 s(-1)) becomes rate-limiting. Our results suggest that all steps on the folding/trimerization pathway of the foldon domain are evolutionarily optimized for rapid and specific initiation of trimer formation during fibritin assembly. The results further show that beta-hairpins allow efficient and rapid protein-protein interactions during folding.
About this Structure
1RFO is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin., Guthe S, Kapinos L, Moglich A, Meier S, Grzesiek S, Kiefhaber T, J Mol Biol. 2004 Apr 2;337(4):905-15. PMID:15033360
Page seeded by OCA on Sun Mar 30 23:27:29 2008
