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Originally published in Science Express on 4 January 2001
Science 19 January 2001: Vol. 291. no. 5503, pp. 498 - 501
DOI: 10.1126/science.1057766
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Reports
Crystal Structure of an Initiation Factor Bound to the 30S Ribosomal Subunit
Andrew P. Carter,1
William M. Clemons Jr.,1
Ditlev E. Brodersen,1
Robert J. Morgan-Warren,1
Thomas Hartsch,2
Brian T. Wimberly,1
V. Ramakrishnan1*
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.
1 Medical Research Council Laboratory of Molecular
Biology, Hills Road, Cambridge CB2 2QH, UK.
2 Göttingen Genomics Laboratory, Institut für
Mikrobiologie und Genetic, Georg-August-Universität
Göttingen, Grisebachstr. 8, D-37077 Göttingen, Germany.
*
To whom correspondence should be addressed. E-mail:
ramak{at}mrc-lmb.cam.ac.uk
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