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Crystal structure of an initiation factor bound to the 30S ribosomal subunit
Author(s): Carter AP, Clemons WM, Brodersen DE, Morgan-Warren RJ, Hartsch T, Wimberly BT, Ramakrishnan V
Source: SCIENCE    Volume: 291    Issue: 5503    Pages: 498-501    Published: JAN 19 2001  
Times Cited: 185     References: 40     
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.
Document Type: Article
Language: English
Reprint Address: Ramakrishnan, V (reprint author), MRC, Mol Biol Lab, Hills Rd, Cambridge CB2 2QH, England
Addresses:
1. MRC, Mol Biol Lab, Cambridge CB2 2QH, England
2. Univ Gottingen, Inst Genet & Mikrobiol, Gottingen Genom Lab, D-37077 Gottingen, Germany
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
Subject Category: Multidisciplinary Sciences
IDS Number: 393UF
ISSN: 0036-8075
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