Crystal structure of a conserved ribosomal protein-RNA complex

被引:241
作者
Conn, GL
Draper, DE
Lattman, EE
Gittis, AG
机构
[1] Johns Hopkins Univ, Dept Chem, Baltimore, MD 21218 USA
[2] Johns Hopkins Univ, Dept Biophys, Baltimore, MD 21218 USA
关键词
D O I
10.1126/science.284.5417.1171
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The structure of a highly conserved complex between a 58-nucleotide domain of Large subunit ribosomal RNA and the RNA-binding domain of ribosomal protein L11 has been solved at 2.8 angstrom resolution. It reveals a precisely folded RNA structure that is stabilized by extensive tertiary contacts and contains an unusually Large core of stacked bases. A bulge Loop base from one hairpin of the RNA is intercalated into the distorted major groove of another helix; the protein Locks this tertiary interaction into place by binding to the intercalated base from the minor groove side. This direct interaction with a key ribosomal RNA tertiary interaction suggests that part of the role of L11 is to stabilize an unusual RNA fold within the ribosome.
引用
收藏
页码:1171 / 1174
页数:4
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