Crystal structure of an initiation factor bound to the 30S ribosomal subunit.

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Carter AP, Clemons WM Jr, Brodersen DE, Morgan-Warren RJ, Hartsch T, Wimberly BT, Ramakrishnan V

Crystal structure of an initiation factor bound to the 30S ribosomal subunit.

Science. 2001 Jan 19;291(5503):498-501.

PubMed ID
11228145 [ View in 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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
30S ribosomal protein S10Q5SHN7Details
30S ribosomal protein S12Q5SHN3Details
30S ribosomal protein S11P80376Details
30S ribosomal protein S13P80377Details
30S ribosomal protein S15Q5SJ76Details
30S ribosomal protein S16Q5SJH3Details
30S ribosomal protein S18Q5SLQ0Details
30S ribosomal protein S19Q5SHP2Details
30S ribosomal protein S20P80380Details
30S ribosomal protein S4P80373Details
30S ribosomal protein S5Q5SHQ5Details
30S ribosomal protein S6Q5SLP8Details
30S ribosomal protein S7P17291Details
30S ribosomal protein S9P80374Details
30S ribosomal protein ThxQ5SIH3Details
30S ribosomal protein S2P80371Details
30S ribosomal protein S3P80372Details
30S ribosomal protein S14 type ZP0DOY6Details
30S ribosomal protein S17P0DOY7Details
30S ribosomal protein S8P0DOY9Details