Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction.

doi:10.1016/j.jmb.2007.09.061

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Article

Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction.

Journal of molecular biology - 11 Jan 2008

Chandrasekar Sowmya, Chartron Justin, Jaru-Ampornpan Peera, Shan Shu-ou

Abstract excerpt

The signal recognition particle (SRP) pathway mediates co-translational targeting of nascent proteins to membranes. Chloroplast SRP is unique in that it does not contain the otherwise universally conserved SRP RNA, which accelerates the association between the SRP guanosine-5'-triphosphate (GTP) binding protein and its receptor FtsY in classical SRP pathways. Recently, we showed that the SRP and SRP receptor (SR)...

Topics

Amino Acid Motifs
Amino Acid Sequence
Arabidopsis
Binding Sites
Chloroplasts
Conserved Sequence
Crystallography, X-Ray
GTP Phosphohydrolases
Hydrogen Bonding
Hydrolysis
Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Malonates

Models, Molecular

Molecular Sequence Data

Mutation

Protein Conformation

Protein Structure, Secondary

Protein Structure, Tertiary

Source

Open in PubMed

Identifiers

PMID: 18035371
DOI: 10.1016/j.jmb.2007.09.061

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Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction.PMID 18035371Read ↗

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