Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor

Leandro F Estrozi; Daniel Boehringer; Shu-Ou Shan; Nenad Ban; Christiane Schaffitzel

doi:10.1038/nsmb.1952

Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor

Leandro F Estrozi, Daniel Boehringer, Shu-Ou Shan, Nenad Ban, Christiane Schaffitzel

School of Biochemistry

Research output: Contribution to journal › Article (Academic Journal) › peer-review

58 Citations (Scopus)

Abstract

We report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM. FtsY binds to the tetraloop of the SRP RNA, whereas the NG domains of the SRP protein and FtsY interact weakly in this conformation. Our results suggest that optimal positioning of the SRP RNA tetraloop and the Ffh NG domain leads to FtsY recruitment.

Original language	English
Pages (from-to)	88-90
Number of pages	3
Journal	Nature Structural and Molecular Biology
Volume	18
Issue number	1
DOIs	https://doi.org/10.1038/nsmb.1952
Publication status	Published - Jan 2011

Keywords

Bacterial Proteins
Cryoelectron Microscopy
Escherichia coli
Escherichia coli Proteins
Models, Molecular
Protein Biosynthesis
Protein Structure, Tertiary
Receptors, Cytoplasmic and Nuclear
Receptors, Peptide
Ribosomes
Signal Recognition Particle

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title = "Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor",

abstract = "We report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM. FtsY binds to the tetraloop of the SRP RNA, whereas the NG domains of the SRP protein and FtsY interact weakly in this conformation. Our results suggest that optimal positioning of the SRP RNA tetraloop and the Ffh NG domain leads to FtsY recruitment.",

keywords = "Bacterial Proteins, Cryoelectron Microscopy, Escherichia coli, Escherichia coli Proteins, Models, Molecular, Protein Biosynthesis, Protein Structure, Tertiary, Receptors, Cytoplasmic and Nuclear, Receptors, Peptide, Ribosomes, Signal Recognition Particle",

author = "Estrozi, {Leandro F} and Daniel Boehringer and Shu-Ou Shan and Nenad Ban and Christiane Schaffitzel",

year = "2011",

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doi = "10.1038/nsmb.1952",

language = "English",

volume = "18",

pages = "88--90",

journal = "Nature Structural and Molecular Biology",

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T1 - Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor

AU - Estrozi, Leandro F

AU - Boehringer, Daniel

AU - Shan, Shu-Ou

AU - Ban, Nenad

AU - Schaffitzel, Christiane

PY - 2011/1

Y1 - 2011/1

N2 - We report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM. FtsY binds to the tetraloop of the SRP RNA, whereas the NG domains of the SRP protein and FtsY interact weakly in this conformation. Our results suggest that optimal positioning of the SRP RNA tetraloop and the Ffh NG domain leads to FtsY recruitment.

AB - We report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM. FtsY binds to the tetraloop of the SRP RNA, whereas the NG domains of the SRP protein and FtsY interact weakly in this conformation. Our results suggest that optimal positioning of the SRP RNA tetraloop and the Ffh NG domain leads to FtsY recruitment.

KW - Bacterial Proteins

KW - Cryoelectron Microscopy

KW - Escherichia coli

KW - Escherichia coli Proteins

KW - Models, Molecular

KW - Protein Biosynthesis

KW - Protein Structure, Tertiary

KW - Receptors, Cytoplasmic and Nuclear

KW - Receptors, Peptide

KW - Ribosomes

KW - Signal Recognition Particle

U2 - 10.1038/nsmb.1952

DO - 10.1038/nsmb.1952

M3 - Article (Academic Journal)

C2 - 21151118

VL - 18

SP - 88

EP - 90

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 1

ER -