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 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.
Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge   CB2 2QH, UK.
A P
AP
Carter
W M
WM
Clemons
D E
DE
Brodersen
R J
RJ
Morgan-Warren
T
T
Hartsch
B T
BT
Wimberly
V
V
Ramakrishnan
D020029:Base Pairing; D001665:Binding Sites; D018360:Crystallography, X-Ray; D015977:Eukaryotic Initiation Factor-1 / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012336:RNA, Ribosomal, 16S / Q000737:chemistry* / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism; D016963:Thermus thermophilus / Q000737:chemistry*
D015977:Eukaryotic Initiation Factor-1; D012336:RNA, Ribosomal, 16S; D012269:Ribosomal Proteins; D012343:RNA, Transfer