DOI: 10.1261/rna.5120503. Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit

Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit

10.1261/rna.5120503

Crossref journal-article

Cold Spring Harbor Laboratory

RNA (246)

Abstract

During translation, tRNAs cycle through three binding sites on the ribosome: the A, the P, and the E sites. We have determined the structures of complexes between the Haloarcula marismortui large ribosomal subunit and two different E site substrates: a deacylated tRNA acceptor stem minihelix and a CCA-acceptor end. Both of these tRNA mimics contain analogs of adenosine 76, the component responsible for a large proportion of E site binding affinity. They bind in the center of the loop-extension of protein L44e, and make specific contacts with both L44e and 23S rRNA including bases that are conserved in all three kingdoms of life. These contacts are consistent with the footprinting, protection, and cross-linking data that have identified the E site biochemically. These structures explain the specificity of the E site for deacylated tRNAs, as it is too small to accommodate any relevant aminoacyl-tRNA. The orientation of the minihelix suggests that it may mimic the P/E hybrid state. It appears that the E site on the 50S subunit was formed by only RNA in the last common ancestor of the three kingdoms, since the proteins at the E sites of H. marismortui and Deinucoccus radiodurans large subunits are not homologous.

Bibliography

SCHMEING, T. M., MOORE, P. B., & STEITZ, T. A. (2003). Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. RNA, 9(11), 1345â1352.

Authors 3

T. MARTIN SCHMEING (first)
PETER B. MOORE (additional)
THOMAS A. STEITZ (additional)

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Dates

Type	When
Created	21 years, 10 months ago (Oct. 15, 2003, 1:38 p.m.)
Deposited	3 years, 9 months ago (Nov. 21, 2021, 8:36 a.m.)
Indexed	1 year ago (Aug. 12, 2024, 7:49 a.m.)
Issued	21 years, 10 months ago (Oct. 15, 2003)
Published	21 years, 10 months ago (Oct. 15, 2003)
Published Online	21 years, 10 months ago (Oct. 15, 2003)
Published Print	21 years, 9 months ago (Nov. 1, 2003)

Funders 0

None

BibTeX

@article{SCHMEING_2003, title={Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit}, volume={9}, ISSN={1469-9001}, url={http://dx.doi.org/10.1261/rna.5120503}, DOI={10.1261/rna.5120503}, number={11}, journal={RNA}, publisher={Cold Spring Harbor Laboratory}, author={SCHMEING, T. MARTIN and MOORE, PETER B. and STEITZ, THOMAS A.}, year={2003}, month=oct, pages={1345–1352} }

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  "abstract": "<jats:p>During translation, tRNAs cycle through three binding sites on the ribosome: the A, the P, and the E sites. We have determined the structures of complexes between the <jats:italic>Haloarcula marismortui</jats:italic> large ribosomal subunit and two different E site substrates: a deacylated tRNA acceptor stem minihelix and a CCA-acceptor end. Both of these tRNA mimics contain analogs of adenosine 76, the component responsible for a large proportion of E site binding affinity. They bind in the center of the loop-extension of protein L44e, and make specific contacts with both L44e and 23S rRNA including bases that are conserved in all three kingdoms of life. These contacts are consistent with the footprinting, protection, and cross-linking data that have identified the E site biochemically. These structures explain the specificity of the E site for deacylated tRNAs, as it is too small to accommodate any relevant aminoacyl-tRNA. The orientation of the minihelix suggests that it may mimic the P/E hybrid state. It appears that the E site on the 50S subunit was formed by only RNA in the last common ancestor of the three kingdoms, since the proteins at the E sites of <jats:italic>H. marismortui</jats:italic> and <jats:italic>Deinucoccus radiodurans</jats:italic> large subunits are not homologous.</jats:p>",
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