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PMID: 8306963 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein.

The EMBO journal ·Vol. 13 ·No. 1 ·1994-01-01 ·Pages 205-12

Hoffman DW, Davies C, Gerchman SE, Kycia JH, Porter SJ, White SW, Ramakrishnan V

Abstract

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).

MeSH Terms
Amino Acid Sequence Crystallography, X-Ray Geobacillus stearothermophilus Models, Molecular Molecular Sequence Data Protein Conformation RNA-Binding Proteins/chemistry Ribosomal Proteins/chemistry
Chemicals
RNA-Binding Proteins Ribosomal Proteins ribosomal protein L9
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Hoffman D W
Department of Microbiology, Duke University Medical Center, Durham, NC 27710.
Davies C
Gerchman S E
Kycia J H
Porter S J
White S W
Ramakrishnan V
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1994-01-01
Pages
205-12
Language
English
Region
England
NLM ID
8208664
PMCID
PMC394794
Subset
IM
Grants
NIGMS NIH HHS · GM 44973 · United States
External Links
PubMed source PMC Full Text View journal details
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