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

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Science  19 Jan 2001:
Vol. 291, Issue 5503, pp. 498-501
DOI: 10.1126/science.1057766

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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.

  • * To whom correspondence should be addressed. E-mail: ramak{at}mrc-lmb.cam.ac.uk

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