Signal recognition particle receptor exposes the ribosomal translocon binding site

Science

Volumn 312, Issue 5774, 2006, Pages 745-747

  Halic, Mario ^a   Gartmann, Marco ^a   Schlenker, Oliver ^b   Mielke, Thorsten ^c   Pool, Martin R ^d   Sinning, Irmgard ^b   Beckmann, Roland ^a,c,e  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^b UNIVERSITY OF HEIDELBERG   (Germany)

^c MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

^d UNIVERSITY OF MANCHESTER   (United Kingdom)

^e UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ELECTRON MICROSCOPY; MEMBRANES; PROTEINS;

CRYO-ELECTRON MICROSCOPY; SIGNAL RECOGNITION PARTICLE; SRP RECEPTOR;

SIGNAL RECONSTRUCTION;

DOCKING PROTEIN; MEMBRANE PROTEIN; SECRETORY PROTEIN; SIGNAL PEPTIDE; SIGNAL RECOGNITION PARTICLE; TRANSLOCON;

CELL ORGANELLE; ELECTRON MICROSCOPY; MEMBRANE; PROTEIN; SIGNAL;

ALU SEQUENCE; ARTICLE; BINDING SITE; CELL MEMBRANE; CRYOELECTRON MICROSCOPY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; RIBOSOME; RNA TRANSLATION; SIGNAL TRANSDUCTION;

ANIMALS; BINDING SITES; CRYOELECTRON MICROSCOPY; DOGS; GUANOSINE TRIPHOSPHATE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECEPTORS, PEPTIDE; RIBOSOMES; SIGNAL RECOGNITION PARTICLE;

EID: 33646442605     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1124864     Document Type: Article

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30. We thank G. Bozkurt for preparation of the mutant SR (SRβ H119A).This work was supported by grants from the VolkswagenStiftung (R.B.) and the Deutsche Forschungsgemeinschaft SFB449 (R.B.) and SFB638 (I.S.); by the Royal Society (M.R.P.); and by the European Union and Senatsverwaltung für Wissenschaft, Forschung und Kultur Berlin (UltraStructureNetwork). Coordinates have been deposited in the RCSB (Research Collaboratory for Structural Bioinformatics) Protein Data Bank with accession number 2G05. The cryo-EM map has been deposited at the 3D-EM database (European Molecular Biology Laboratory-European Bioinformatics Institute, Cambridge, UK) with accession number EMD-1217.