1rfo

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{{STRUCTURE_1rfo| PDB=1rfo | SCENE= }}
{{STRUCTURE_1rfo| PDB=1rfo | SCENE= }}
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'''Trimeric Foldon of the T4 phagehead fibritin'''
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===Trimeric Foldon of the T4 phagehead fibritin===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15033360 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15033360}}
==About this Structure==
==About this Structure==
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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].
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1RFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFO OCA].
==Reference==
==Reference==
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[[Category: Beta hairpin]]
[[Category: Beta hairpin]]
[[Category: Trimer]]
[[Category: Trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:19:46 2008''

Revision as of 07:19, 29 July 2008

Image:1rfo.png

Template:STRUCTURE 1rfo

Trimeric Foldon of the T4 phagehead fibritin

Template:ABSTRACT PUBMED 15033360

About this Structure

1RFO is a Single protein structure of sequence from Enterobacteria phage t4. Full experimental 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

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