期刊
ELIFE
卷 5, 期 -, 页码 -出版社
eLIFE SCIENCES PUBL LTD
DOI: 10.7554/eLife.20718
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资金
- Botechnology and Biological Sciences Research Council [BB/L002531/1, BB/I019855/1]
- Wellcome [107929/Z/15/Z, 110183/Z/15/Z]
- Medical Research Council [G1001640]
- European Commission [626436]
- Wellcome Trust [107929/Z/15/Z, 110183/Z/15/Z] Funding Source: Wellcome Trust
- BBSRC [BB/I019855/1, BB/H018050/1, BB/L002531/1, BB/L001306/1] Funding Source: UKRI
- MRC [G1001640] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L001306/1, BB/I019855/1, BB/L002531/1, BB/H018050/1] Funding Source: researchfish
- Medical Research Council [G1001640] Funding Source: researchfish
- Wellcome Trust [107929/Z/15/Z] Funding Source: researchfish
The twin-arginine protein translocation system (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membranes of plant chloroplasts. The Tat transporter is assembled from multiple copies of the membrane proteins TatA, TatB, and TatC. We combine sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between the Tat proteins of Escherichia coli at molecular-level resolution. In the TatBC receptor complex the transmembrane helix of each TatB molecule is sandwiched between two TatC molecules, with one of the inter-subunit interfaces incorporating a functionally important cluster of interacting polar residues. Unexpectedly, we find that TatA also associates with TatC at the polar cluster site. Our data provide a structural model for assembly of the active Tat translocase in which substrate binding triggers replacement of TatB by TatA at the polar cluster site. Our work demonstrates the power of co-evolution analysis to predict protein interfaces in multi-subunit complexes.
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