YidC from Escherichia coli Forms an Ion-Conducting Pore upon Activation by Ribosomes
YidC from Escherichia coli Forms an Ion-Conducting Pore upon Activation by Ribosomes
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Publisher
Switzerland: MDPI AG
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Language
English
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Publisher
Switzerland: MDPI AG
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Contents
The universally conserved protein YidC aids in the insertion and folding of transmembrane polypeptides. Supposedly, a charged arginine faces its hydrophobic lipid core, facilitating polypeptide sliding along YidC’s surface. How the membrane barrier to other molecules may be maintained is unclear. Here, we show that the purified and reconstituted E....
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YidC from Escherichia coli Forms an Ion-Conducting Pore upon Activation by Ribosomes
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TN_cdi_doaj_primary_oai_doaj_org_article_4a5b2448fb7b4c3581e73361d01c6d93
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_4a5b2448fb7b4c3581e73361d01c6d93
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ISSN
2218-273X
E-ISSN
2218-273X
DOI
10.3390/biom13121774
