2ihr
From Proteopedia
(New page: 200px<br /><applet load="2ihr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ihr, resolution 2.5Å" /> '''RF2 of Thermus thermo...) |
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==Overview== | ==Overview== | ||
| - | Prokaryotic class I release factors (RFs) respond to mRNA stop codons and | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Release | + | Release factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies., Zoldak G, Redecke L, Svergun DI, Konarev PV, Voertler CS, Dobbek H, Sedlak E, Sprinzl M, Nucleic Acids Res. 2007;35(4):1343-53. Epub 2007 Feb 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17272297 17272297] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Dobbek, H.]] | [[Category: Dobbek, H.]] | ||
[[Category: Sprinzl, M.]] | [[Category: Sprinzl, M.]] | ||
| - | [[Category: Voertler, C | + | [[Category: Voertler, C S.]] |
[[Category: mixed alpha-beta]] | [[Category: mixed alpha-beta]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:49 2008'' |
Revision as of 15:52, 21 February 2008
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RF2 of Thermus thermophilus
Overview
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.
About this Structure
2IHR is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Release factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies., Zoldak G, Redecke L, Svergun DI, Konarev PV, Voertler CS, Dobbek H, Sedlak E, Sprinzl M, Nucleic Acids Res. 2007;35(4):1343-53. Epub 2007 Feb 1. PMID:17272297
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