1div
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(New page: 200px<br /><applet load="1div" size="450" color="white" frame="true" align="right" spinBox="true" caption="1div, resolution 2.6Å" /> '''RIBOSOMAL PROTEIN L9'...)
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Revision as of 11:11, 20 November 2007
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RIBOSOMAL PROTEIN L9
Overview
The crystal structure of protein L9 from the Bacillus stearothermophilus, ribosome has been determined at 2.8 A resolution using X-ray diffraction, methods. This primary RNA-binding protein has a highly elongated and, unusual structure consisting of two separated domains joined by a long, exposed alpha-helix. Conserved, positively charged and aromatic amino, acids on the surfaces of both domains probably represent the sites of, specific interactions with 23S rRNA. Comparisons with other prokaryotic L9, sequences show that while the length of the connecting alpha-helix is, invariant, the sequence within the exposed central region is not, conserved. This suggests that the alpha-helix has an architectural role, and serves to fix the relative separation and orientation of the N- and, C-terminal domains within the ribosome. The N-terminal domain has, structural homology to the smaller ribosomal proteins L7/L12 and L30, and, the eukaryotic RNA recognition motif (RRM).
About this Structure
1DIV is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein., Hoffman DW, Davies C, Gerchman SE, Kycia JH, Porter SJ, White SW, Ramakrishnan V, EMBO J. 1994 Jan 1;13(1):205-12. PMID:8306963
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