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Article

Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation.

Proceedings of the National Academy of Sciences of the United States of America - 11 Jun 2013

Moser Michael, Nagamori Shushi, Huber Maria, Tokuda Hajime, Nishiyama Ken-ichi

Abstract excerpt

Presecretory proteins are translocated across biological membranes through protein-conducting channels such as Sec61 (eukaryotes) and SecYEG (bacteria). SecA, a translocation ATPase, pushes preproteins out with dynamic structural changes through SecYEG. SecG, a subunit of the SecYEG channel possessing two transmembrane stretches (TMs), undergoes topology inversion coupled with SecA-dependent translocation....

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Share to Bacterial Outer Membrane Proteins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 23716687
DOI: 10.1073/pnas.1303160110
PMCID: PMC3683788

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Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation.PMID 23716687Read ↗

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Features of membrane protein sequence direct post-translational insertion.Semantic proximity Read ↗

Translocation of proteins through the Sec61 and SecYEG channels.Semantic proximity Read ↗

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Dimeric SecA is essential for protein translocation.Semantic proximity Read ↗

The SecY translocation complex: convergence of genetics and structure.Semantic proximity Read ↗

Roles of SecG in ATP- and SecA-dependent protein translocation.Semantic proximity Read ↗

Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA.Semantic proximity Read ↗

Nearest neighbor analysis of the SecYEG complex. 1. Identification of a SecY-SecG interface.Semantic proximity Read ↗

Unlocking the Bacterial SecY Translocon.Semantic proximity Read ↗

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