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PMID: 8635468 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus.

The EMBO journal ·Vol. 15 ·No. 6 ·1996-03-15 ·Pages 1350-9

Nikonov S, Nevskaya N, Eliseikina I, Fomenkova N, Nikulin A, Ossina N, Garber M, Jonsson BH, Briand C, Al-Karadaghi S, Svensson A, Aevarsson A, Liljas A

Abstract

L1 has a dual function as a ribosomal protein binding rRNA and as a translational repressor binding mRNA. The crystal structure of L1 from Thermus thermophilus has been determined at 1.85 angstroms resolution. The protein is composed of two domains with the N- and C-termini in domain I. The eight N-terminal residues are very flexible, as the quality of electron density map shows. Proteolysis experiments have shown that the N-terminal tail is accessible and important for 23S rRNA binding. Most of the conserved amino acids are situated at the interface between the two domains. They probably form the specific RNA binding site of L1. Limited non-covalent contacts between the domains indicate an unstable domain interaction in the present conformation. Domain flexibility and RNA binding by induced fit seems plausible.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/chemistry Base Sequence Consensus Sequence Crystallography, X-Ray Models, Molecular Molecular Sequence Data Protein Conformation RNA-Binding Proteins/chemistry Ribosomal Proteins/chemistry Sequence Homology, Amino Acid Structure-Activity Relationship Thermus thermophilus/chemistry
Chemicals
Bacterial Proteins RNA-Binding Proteins Ribosomal Proteins ribosomal protein L1
Authors & Affiliations
13 authors, click to expand affiliations / ORCID
Nikonov S
Department of Structure and Function of Ribosomes, Russian Academy of Sciences, Russia.
Nevskaya N
Eliseikina I
Fomenkova N
Nikulin A
Ossina N
Garber M
Jonsson B H
Briand C
Al-Karadaghi S
Svensson A
Aevarsson A
Liljas A
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1996-03-15
Pages
1350-9
Language
English
Region
England
NLM ID
8208664
PMCID
PMC450039
Subset
IM
Databases
GENBANK
P02384, P04447, P05966, P09764, P10054, P12738, P13575, P15824, P27150, P29393, P35024, P36236, P36248, P36256, P41199, Q07976
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PubMed source PMC Full Text View journal details
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