Spirin A S
FEBS Lett. 1983 Jun 13;156(2):217-21. doi: 10.1016/0014-5793(83)80499-2.
Electron microscopy results of Lake [J. Mol. Biol. (1976) 105, 131-159] and Vasiliev et al. [FEBS Lett. (1983) 155, 167-172] suggest that the 70 S ribosome has an open pocket or a cavity at the base of the L7/L12 stalk of the 50 S subunit, on the side of the 30 S subunit opposite to its bulge or platform. It is this pocket that is proposed here to be the site for binding and retention of two L-shaped tRNA molecules on the ribosome. The model proposed is consistent with the facts about interactions of the protein L7/L12 with the elongation factors (EF-Tu and EF-G) involved in tRNA binding and translocation, as well as with the data available on the participation of proteins S3, S5, S10, S14 and S19 in the formation of tRNA sites.
莱克[《分子生物学杂志》（1976年）第105卷，第131 - 159页]以及瓦西里耶夫等人[《欧洲生物化学学会联合会快报》（1983年）第155卷，第167 - 172页]的电子显微镜结果表明，70S核糖体在50S亚基的L7/L12茎底部有一个开放口袋或腔，位于30S亚基与凸起或平台相对的一侧。本文提出正是这个口袋是核糖体上两个L形tRNA分子结合和保留的位点。所提出的模型与蛋白质L7/L12与参与tRNA结合和易位的延伸因子（EF - Tu和EF - G）相互作用的事实一致，也与蛋白质S3、S5、S10、S14和S19参与tRNA位点形成的现有数据一致。
