Crystal Structure of an Initiation Factor Bound to the 30S Ribosomal Subunit

Initiation of translation at the correct position on messenger RNA is essential for accurate protein synthesis. In prokaryotes, this process requires three initiation factors: IF1, IF2, and IF3. Here we report the crystal structure of a complex of IF1 and the 30S ribosomal subunit. Binding of IF1 oc...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2001-01, Vol.291 (5503), p.498-501
Main Authors: Carter, Andrew P., Clemons, William M., Brodersen, Ditlev E., Morgan-Warren, Robert J., Hartsch, Thomas, Wimberly, Brian T., Ramakrishnan, V.
Format: Article
Language:English
Subjects:
Base Pairing
Binding Sites
Biochemical genetics
Biochemistry
Biological and medical sciences
Coordinate systems
Crystal structure
Crystalline structure
Crystallography
Crystallography, X-Ray
Crystals
Escherichia coli
Eukaryotic Initiation Factor-1 - chemistry
Eukaryotic Initiation Factor-1 - metabolism
Fundamental and applied biological sciences. Psychology
Genes
Hydrogen Bonding
Inhalants
Medical research
Messenger RNA
Models, Molecular
Molecular biophysics
Molecular structure
Nucleic Acid Conformation
Observation
Peptide initiation factors
Protein Conformation
Protein Structure, Secondary
Proteins
Ribonucleic acid
Ribosomal Proteins - chemistry
Ribosomal Proteins - metabolism
ribosomal subunit 30S
Ribosomes
Ribosomes - chemistry
Ribosomes - metabolism
RNA
RNA, Ribosomal, 16S - chemistry
RNA, Ribosomal, 16S - metabolism
RNA, Transfer - metabolism
Structure in molecular biology
Thermus thermophilus - chemistry
transcription initiation factor IF1
Transfer RNA
Translation
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Summary:Initiation of translation at the correct position on messenger RNA is essential for accurate protein synthesis. In prokaryotes, this process requires three initiation factors: IF1, IF2, and IF3. Here we report the crystal structure of a complex of IF1 and the 30S ribosomal subunit. Binding of IF1 occludes the ribosomal A site and flips out the functionally important bases A1492 and A1493 from helix 44 of 165 RNA, burying them in pockets in IF1. The binding of IF1 causes long-range changes in the conformation of H44 and leads to movement of the domains of 30S with respect to each other. The structure explains how localized changes at the ribosomal A site lead to global alterations in the conformation of the 305 subunit.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1057766