2aki

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2aki

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Normal mode-based flexible fitted coordinates of a translocating SecYEG protein-conducting channel into the cryo-EM map of a SecYEG-nascent chain-70S ribosome complex from E. coli

Overview

Secreted and membrane proteins are translocated across or into cell, membranes through a protein-conducting channel (PCC). Here we present a, cryo-electron microscopy reconstruction of the Escherichia coli PCC, SecYEG, complexed with the ribosome and a nascent chain containing a, signal anchor. This reconstruction shows a messenger RNA, three transfer, RNAs, the nascent chain, and detailed features of both a translocating PCC, and a second, non-translocating PCC bound to mRNA hairpins. The, translocating PCC forms connections with ribosomal RNA hairpins on two, sides and ribosomal proteins at the back, leaving a frontal opening., Normal mode-based flexible fitting of the archaeal SecYEbeta structure, into the PCC electron microscopy densities favours a front-to-front, arrangement of two SecYEG complexes in the PCC, and supports channel, formation by the opening of two linked SecY halves during polypeptide, translocation. On the basis of our observation in the translocating PCC of, two segregated pores with different degrees of access to bulk lipid, we, propose a model for co-translational protein translocation.

About this Structure

2AKI is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the E. coli protein-conducting channel bound to a translating ribosome., Mitra K, Schaffitzel C, Shaikh T, Tama F, Jenni S, Brooks CL 3rd, Ban N, Frank J, Nature. 2005 Nov 17;438(7066):318-24. PMID:16292303

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