1whi
From Proteopedia
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RIBOSOMAL PROTEIN L14
Overview
BACKGROUND: Detailed structural information on ribosomal proteins has, increased our understanding of the structure, function and evolution of, the ribosome. L14 is one of the most conserved ribosomal proteins and, appears to have a central role in the ribonucleoprotein complex. Studies, have indicated that L14 occupies a central location between the peptidyl, transferase and GTPase regions of the large ribosomal subunit. RESULTS:, The crystal structure of L14 from Bacillus stearothermophilus has been, solved using a combination of isomorphous replacement and multiwavelength, anomalous dispersion (MAD) methods. The structure comprises a, five-stranded beta-barrel, a C-terminal loop region that contains two, small alpha-helices, and a beta-ribbon that projects from the beta-barrel., An analysis of the structure and the conserved amino acids reveals three, surface patches that probably mediate L14-RNA and L14-protein interactions, within the ribosome. CONCLUSIONS: The accepted role of ribosomal proteins, is to promote the folding and stabilization of ribosomal RNA. The L14, structure is consistent with this notion, and it suggests that the RNA, binds in two sites. One RNA-binding site appears to recognize a distinct, region of ribosomal RNA during particle assembly. The second site is, smaller and may become occupied during the later compaction of the RNA., The surface hydrophobic patch is a likely site of protein-protein, interaction, possibly with L19.
About this Structure
1WHI is a Single protein structure of sequence from Geobacillus stearothermophilus. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
The crystal structure of ribosomal protein L14 reveals an important organizational component of the translational apparatus., Davies C, White SW, Ramakrishnan V, Structure. 1996 Jan 15;4(1):55-66. PMID:8805509
Page seeded by OCA on Tue Dec 18 18:38:50 2007
