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| [[Image:2ihr.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2ihr| PDB=2ihr | SCENE= }} | | {{STRUCTURE_2ihr| PDB=2ihr | SCENE= }} |
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| '''RF2 of Thermus thermophilus'''
| | ===RF2 of Thermus thermophilus=== |
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| ==Overview==
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| Prokaryotic class I release factors (RFs) respond to mRNA stop codons and terminate protein synthesis. They interact with the ribosomal decoding site and the peptidyl-transferase centre bridging these 75 A distant ribosomal centres. For this an elongated RF conformation, with partially unfolded core domains II.III.IV is required, which contrasts the known compact RF crystal structures. The crystal structure of Thermus thermophilus RF2 was determined and compared with solution structure of T. thermophilus and Escherichia coli RF2 by microcalorimetry, circular dichroism spectroscopy and small angle X-ray scattering. The structure of T. thermophilus RF2 in solution at 20 degrees C is predominantly compact like the crystal structure. Thermodynamic analysis point to an initial melting of domain I, which is independent from the melting of the core. The core domains II.III.IV melt cooperatively at the respective physiological temperatures for T. thermophilus and E. coli. Thermodynamic analyses and the X-ray scattering results for T. thermophilus RF2 in solution suggest that the compact conformation of RF2 resembles a physiological state in absence of the ribosome.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17272297}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17272297 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17272297}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Voertler, C S.]] | | [[Category: Voertler, C S.]] |
| [[Category: Mixed alpha-beta]] | | [[Category: Mixed alpha-beta]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:31:09 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:31:42 2008'' |
