《Nature》目录要览：2010-12-02出版
时间：2010-12-02 阅读： 我要评论:
Article: http://www.nature.com/nature/journal/v468/n7324/full/nature09555.html
Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites pp713 - 716
During translation, tRNAs enter the ribosome and then move sequentially through three sites, known as A, P and E, as they transfer their attached amino acids onto the growing peptide chain. How the ribosome facilitates tRNA translocation between the sites remains largely unknown. Now a study uses multiparticle cryoelectron microscopy of a ribosome bound to the translation elongation factor, EF-G, to get information about tRNA movement. It identifies two new substates and sees that translocation is linked to unratcheting of the 30S ribosomal subunit.
Andreas H. Ratje et al.
doi:10.1038/nature09547
Abstract: http://www.nature.com/nature/journal/v468/n7324/abs/nature09547.html
Article: http://www.nature.com/nature/journal/v468/n7324/full/nature09547.html
Structure and mechanism of the S component of a bacterial ECF transporter pp717 - 720
The energy-coupling factor transporters are responsible for vitamin uptake in prokaryotes. Here, the X-ray crystal structure of the membrane-embedded, substrate-binding domain of a riboflavin transporter from Staphylococcus aureus is reported. The transporter adopts a previously unreported fold and contains a riboflavin molecule bound to a loop and the periplasmic portion of several transmembrane segments.
Peng Zhang, Jiawei Wang and Yigong Shi
doi:10.1038/nature09488
Abstract: http://www.nature.com/nature/journal/v468/n7324/abs/nature09488.html
Article: http://www.nature.com/nature/journal/v468/n7324/full/nature09488.html
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来源：Nature 作者：Environmentor （环境人 Environmentor.Cn）
