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Article

A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor.

Journal of molecular biology - 28 Mar 2008

Weiche Benjamin, Bürk Jonas, Angelini Sandra, Schiltz Emile, Thumfart Jörg Oliver, Koch Hans-Georg

Abstract excerpt

Different from eukaryotes, the bacterial signal recognition particle (SRP) receptor lacks a membrane-tethering SRP receptor (SR) beta subunit and is composed of only the SR alpha homologue FtsY. FtsY is a modular protein composed of three domains. The N- and G-domains of FtsY are highly similar to the corresponding domains of Ffh/SRP54 and SR alpha and constitute the essential core of FtsY. In contrast, the...

Topics

Amino Acid Sequence
Bacterial Proteins
Cell Membrane
Escherichia coli
Escherichia coli Proteins
Molecular Sequence Data
Mutation
Protein Isoforms
Protein Structure, Tertiary
Receptors, Cytoplasmic and Nuclear

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Receptors, Peptide

Signal Recognition Particle

Source

Identifiers

PMID: 18281057
DOI: 10.1016/j.jmb.2008.01.040

Genes

SRP54

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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