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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6019
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pubmed:dateCreated |
2011-2-18
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4.5S RNA,
http://linkedlifedata.com/resource/pubmed/chemical/5'-guanylylmethylenebisphosphonate,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ffh protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/FtsY protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Signal Recognition Particle,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein L23, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein L29
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
331
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
881-6
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pubmed:dateRevised |
2011-10-18
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pubmed:meshHeading |
pubmed-meshheading:21330537-Bacterial Proteins,
pubmed-meshheading:21330537-Base Sequence,
pubmed-meshheading:21330537-Binding Sites,
pubmed-meshheading:21330537-Crystallization,
pubmed-meshheading:21330537-Crystallography, X-Ray,
pubmed-meshheading:21330537-Enzyme Activation,
pubmed-meshheading:21330537-Escherichia coli,
pubmed-meshheading:21330537-Escherichia coli Proteins,
pubmed-meshheading:21330537-GTP Phosphohydrolases,
pubmed-meshheading:21330537-Guanosine Triphosphate,
pubmed-meshheading:21330537-Hydrogen Bonding,
pubmed-meshheading:21330537-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:21330537-Models, Biological,
pubmed-meshheading:21330537-Models, Molecular,
pubmed-meshheading:21330537-Nucleic Acid Conformation,
pubmed-meshheading:21330537-Protein Conformation,
pubmed-meshheading:21330537-Protein Multimerization,
pubmed-meshheading:21330537-Protein Structure, Tertiary,
pubmed-meshheading:21330537-Protein Transport,
pubmed-meshheading:21330537-RNA, Bacterial,
pubmed-meshheading:21330537-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:21330537-Ribosomal Proteins,
pubmed-meshheading:21330537-Ribosomes,
pubmed-meshheading:21330537-Signal Recognition Particle
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pubmed:year |
2011
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pubmed:articleTitle |
The crystal structure of the signal recognition particle in complex with its receptor.
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pubmed:affiliation |
Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich (ETH Zurich), Zurich, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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