Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-Å resolution

Min Lu, Thomas A. Steitz

Research output: Contribution to journalArticle

82 Citations (Scopus)

Abstract

The crystal structure of Escherichia coli ribosomal protein L25 bound to an 18-base pair portion of 5S ribosomal RNA, which contains "loop E," has been determined at 1.8-Å resolution. The protein primarily recognizes a unique RNA shape, although five side chains make direct or water-mediated interactions with bases. Three β-strands lie in the widened minor groove of loop E formed by noncanonical base pairs and cross-strand purine stacks, and an α-helix interacts in an adjacent widened major groove. The structure of loop E is largely the same as that of uncomplexed RNA (rms deviation of 0.4 Å for 11 base pairs), and 3 Mg2+ ions that stabilize the noncanonical base pairs lie in the same or similar locations in both structures. Perhaps surprisingly, those residues interacting with the RNA backbone are the most conserved among known L25 sequences, whereas those interacting with the bases are not.

Original languageEnglish (US)
Pages (from-to)2023-2028
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume97
Issue number5
DOIs
StatePublished - Feb 29 2000
Externally publishedYes

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Escherichia coli Proteins
Base Pairing
RNA
5S Ribosomal RNA
Ions
ribosomal protein L25
Water
Proteins

All Science Journal Classification (ASJC) codes

  • General

Cite this

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abstract = "The crystal structure of Escherichia coli ribosomal protein L25 bound to an 18-base pair portion of 5S ribosomal RNA, which contains {"}loop E,{"} has been determined at 1.8-{\AA} resolution. The protein primarily recognizes a unique RNA shape, although five side chains make direct or water-mediated interactions with bases. Three β-strands lie in the widened minor groove of loop E formed by noncanonical base pairs and cross-strand purine stacks, and an α-helix interacts in an adjacent widened major groove. The structure of loop E is largely the same as that of uncomplexed RNA (rms deviation of 0.4 {\AA} for 11 base pairs), and 3 Mg2+ ions that stabilize the noncanonical base pairs lie in the same or similar locations in both structures. Perhaps surprisingly, those residues interacting with the RNA backbone are the most conserved among known L25 sequences, whereas those interacting with the bases are not.",
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AU - Steitz, Thomas A.

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N2 - The crystal structure of Escherichia coli ribosomal protein L25 bound to an 18-base pair portion of 5S ribosomal RNA, which contains "loop E," has been determined at 1.8-Å resolution. The protein primarily recognizes a unique RNA shape, although five side chains make direct or water-mediated interactions with bases. Three β-strands lie in the widened minor groove of loop E formed by noncanonical base pairs and cross-strand purine stacks, and an α-helix interacts in an adjacent widened major groove. The structure of loop E is largely the same as that of uncomplexed RNA (rms deviation of 0.4 Å for 11 base pairs), and 3 Mg2+ ions that stabilize the noncanonical base pairs lie in the same or similar locations in both structures. Perhaps surprisingly, those residues interacting with the RNA backbone are the most conserved among known L25 sequences, whereas those interacting with the bases are not.

AB - The crystal structure of Escherichia coli ribosomal protein L25 bound to an 18-base pair portion of 5S ribosomal RNA, which contains "loop E," has been determined at 1.8-Å resolution. The protein primarily recognizes a unique RNA shape, although five side chains make direct or water-mediated interactions with bases. Three β-strands lie in the widened minor groove of loop E formed by noncanonical base pairs and cross-strand purine stacks, and an α-helix interacts in an adjacent widened major groove. The structure of loop E is largely the same as that of uncomplexed RNA (rms deviation of 0.4 Å for 11 base pairs), and 3 Mg2+ ions that stabilize the noncanonical base pairs lie in the same or similar locations in both structures. Perhaps surprisingly, those residues interacting with the RNA backbone are the most conserved among known L25 sequences, whereas those interacting with the bases are not.

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