1HR0

CRYSTAL STRUCTURE OF INITIATION FACTOR IF1 BOUND TO THE 30S RIBOSOMAL SUBUNIT

Summary for 1HR0

• Entry DOI: 10.2210/pdb1hr0/pdb
• Related: 1FJF 1FJG 1QD7
• Descriptor: 16S RIBOSOMAL RNA, 30S RIBOSOMAL PROTEIN S9, 30S RIBOSOMAL PROTEIN S10, ... (25 entities in total)
• Functional Keywords: 30s, ribosomal subunit, ribosome, initiation factor, if1
• Biological source: Escherichia coli; More
• Total number of polymer chains: 23
• Total formula weight: 795153.98

Authors

Carter, A.P.,Clemons Jr., W.M.,Brodersen, D.E.,Morgan-Warren, R.J.,Wimberly, B.T.,Ramakrishnan, V. (deposition date: 2000-12-20, release date: 2001-01-24, Last modification date: 2023-08-09)

Primary citation

Carter, A.P.,Clemons Jr., W.M.,Brodersen, D.E.,Morgan-Warren, R.J.,Hartsch, T.,Wimberly, B.T.,Ramakrishnan, V.
Crystal structure of an initiation factor bound to the 30S ribosomal subunit.
Science, 291:498-501, 2001

PubMed Abstract: 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 16S 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 30S subunit.

PubMed: 11228145
DOI: 10.1126/science.1057766

Experimental method

X-RAY DIFFRACTION (3.2 Å)