1div

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1div FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1div OCA], [http://www.ebi.ac.uk/pdbsum/1div PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1div RCSB]</span>
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[[Category: rrna-binding]]
[[Category: rrna-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:42:25 2008''

Revision as of 16:42, 30 March 2008


PDB ID 1div

Drag the structure with the mouse to rotate
, resolution 2.6Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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