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'''NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, 33 STRUCTURES''' | '''NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, 33 STRUCTURES''' | ||
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[[Category: Markus, M A.]] | [[Category: Markus, M A.]] | ||
[[Category: Torchia, D A.]] | [[Category: Torchia, D A.]] | ||
[[Category: | [[Category: Alpha-helical protein]] | ||
[[Category: | [[Category: Homeodomain fold]] | ||
[[Category: | [[Category: L11-c76]] | ||
[[Category: | [[Category: Ribosomal protein]] | ||
[[Category: | [[Category: Rna-binding domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:35:27 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 16:35, 2 May 2008
NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, 33 STRUCTURES
OverviewOverview
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 StructureAbout this Structure
1FOX is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 16:35:27 2008