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-Structure paper
タイトル | RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors. |
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ジャーナル・号・ページ | Cell, Vol. 129, Issue 5, Page 929-941, Year 2007 |
掲載日 | 2007年6月1日 |
著者 | Haixiao Gao / Zhihong Zhou / Urmila Rawat / Chenhui Huang / Lamine Bouakaz / Chernhoe Wang / Zhihong Cheng / Yuying Liu / Andrey Zavialov / Richard Gursky / Suparna Sanyal / Måns Ehrenberg / Joachim Frank / Haiwei Song / |
PubMed 要旨 | During translation termination, class II release factor RF3 binds to the ribosome to promote rapid dissociation of a class I release factor (RF) in a GTP-dependent manner. We present the crystal ...During translation termination, class II release factor RF3 binds to the ribosome to promote rapid dissociation of a class I release factor (RF) in a GTP-dependent manner. We present the crystal structure of E. coli RF3*GDP, which has a three-domain architecture strikingly similar to the structure of EF-Tu*GTP. Biochemical data on RF3 mutants show that a surface region involving domains II and III is important for distinct steps in the action cycle of RF3. Furthermore, we present a cryo-electron microscopy (cryo-EM) structure of the posttermination ribosome bound with RF3 in the GTP form. Our data show that RF3*GTP binding induces large conformational changes in the ribosome, which break the interactions of the class I RF with both the decoding center and the GTPase-associated center of the ribosome, apparently leading to the release of the class I RF. |
リンク | Cell / PubMed:17540173 |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.8 - 15.5 Å |
構造データ | EMDB-1302: RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors. PDB-2h5e: |
化合物 | ChemComp-GDP: ChemComp-HOH: |
由来 |
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キーワード | TRANSLATION / BETA BARREL / RF3 / Ribosome / cryo-EM |