Crystal Structure of the Ribonucleoprotein Core of the Signal Recognition Particle

• Published in: Science (American Association for the Advancement of Science) Vol. 287; no. 5456; pp. 1232 - 1239
• Main Authors: Batey, Robert T., Rambo, Robert P., Lucast, Louise, Rha, Brian, Doudna, Jennifer A.
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for the Advancement of Science 18-02-2000; American Association for the Advancement of Science; The American Association for the Advancement of Science
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Base Pairing; Binding and carrier proteins; Binding Sites; Biological and medical sciences; Cell growth; Cell Membrane - metabolism; Crystal structure; Crystallography; Crystallography, X-Ray; Crystals; Escherichia coli - chemistry; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins; Fundamental and applied biological sciences. Psychology; Genetics; Guanosine Triphosphate - metabolism; Hydrogen Bonding; Hydrogen bonds; Ions; Literary Devices; Magnesium - metabolism; Models, Molecular; Molecular Sequence Data; Molecules; Nucleic Acid Conformation; Nucleotides; Plasmids; Potassium; Potassium - metabolism; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Proteins; Ribonucleic acid; RNA; RNA, Bacterial - chemistry; RNA, Bacterial - genetics; RNA, Bacterial - metabolism; signal recognition particle; Signal Recognition Particle - chemistry; Signal Recognition Particle - metabolism; Space life sciences; Transformation, Bacterial; Water - metabolism; Intracellular transport; Eucaryote; Ribonucleoprotein; Ribosome; Signal recognition particle; RNA; Nucleotide sequence; Homology; Molecular interaction; Signal transduction; Procaryote; Three dimensional structure; Helical structure; Crystalline structure
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.287.5456.1232

The signal recognition particle (SRP), a protein-RNA complex conserved in all three kingdoms of life, recognizes and transports specific proteins to cellular membranes for insertion or secretion. We describe here the 1.8 angstrom crystal structure of the universal core of the SRP, revealing protein recognition of a distorted RNA minor groove. Nucleotide analog interference mapping demonstrates the biological importance of observed interactions, and genetic results show that this core is functional in vivo. The structure explains why the conserved residues in the protein and RNA are required for SRP assembly and defines a signal sequence recognition surface composed of both protein and RNA.