2XXA

The Crystal Structure of the Signal Recognition Particle (SRP) in Complex with its Receptor(SR)

Summary for 2XXA

• Entry DOI: 10.2210/pdb2xxa/pdb
• Related: 1DUL 1FTS 1HQ1 2J28 2XKV
• Descriptor: SIGNAL RECOGNITION PARTICLE PROTEIN, SRP RECEPTOR FTSY, 4.5S RNA, ... (6 entities in total)
• Functional Keywords: protein transport, rna/rna binding protein, hydrolase, gtpase
• Biological source: ESCHERICHIA COLI K-12; More
• Cellular location: Cytoplasm: P0AGD7; Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P10121
• Total number of polymer chains: 6
• Total formula weight: 232073.68

Authors

Ataide, S.F.,Schmitz, N.,Shen, K.,Ke, A.,Shan, S.,Doudna, J.A.,Ban, N. (deposition date: 2010-11-09, release date: 2011-03-02, Last modification date: 2023-12-20)

Primary citation

Ataide, S.F.,Schmitz, N.,Shen, K.,Ke, A.,Shan, S.,Doudna, J.A.,Ban, N.
The Crystal Structure of the Signal Recognition Particle in Complex with its Receptor.
Science, 331:881-, 2011

PubMed Abstract: Cotranslational targeting of membrane and secretory proteins is mediated by the universally conserved signal recognition particle (SRP). Together with its receptor (SR), SRP mediates the guanine triphosphate (GTP)-dependent delivery of translating ribosomes bearing signal sequences to translocons on the target membrane. Here, we present the crystal structure of the SRP:SR complex at 3.9 angstrom resolution and biochemical data revealing that the activated SRP:SR guanine triphosphatase (GTPase) complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated. Combined with previous findings, these results suggest that the SRP:SR GTPase complex initially assembles at the tetraloop end of the SRP RNA and then relocalizes to the opposite end of the RNA. This rearrangement provides a mechanism for coupling GTP hydrolysis to the handover of cargo to the translocon.

PubMed: 21330537
DOI: 10.1126/SCIENCE.1196473

Experimental method

X-RAY DIFFRACTION (3.94 Å)