1fow
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(New page: 200px<br /><applet load="1fow" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fow" /> '''NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOM...)
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Revision as of 12:59, 20 November 2007
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NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, MINIMIZED AVERAGE STRUCTURE
Overview
The structure of the C-terminal RNA recognition domain of ribosomal, protein L11 has been solved by heteronuclear three-dimensional nuclear, magnetic resonance spectroscopy. Although the structure can be considered, high resolution in the core, 15 residues between helix alpha 1 and strand, beta 1 form an extended, unstructured loop. 15N transverse relaxation, measurements suggest that the loop is moving on a picosecond-to-nanosecond, time scale in the free protein but not in the protein bound to RNA., Chemical shifts differences between the free protein and the bound protein, suggest that the loop as well as the C-terminal end of helix alpha 3 are, involved in RNA binding.
About this Structure
1FOW is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA., Markus MA, Hinck AP, Huang S, Draper DE, Torchia DA, Nat Struct Biol. 1997 Jan;4(1):70-7. PMID:8989327
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