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8 results on '"Pascoa, Tomas C."'

2. The structural basis of fatty acid elongation by the ELOVL elongases

Author

Nie, Laiyin, Pascoa, Tomas C., Pike, Ashley C. W., Bushell, Simon R., Quigley, Andrew, Ruda, Gian Filippo, Chu, Amy, Cole, Victoria, Speedman, David, Moreira, Tiago, Shrestha, Leela, Mukhopadhyay, Shubhashish M. M., Burgess-Brown, Nicola A., Love, James D., Brennan, Paul E., and Carpenter, Elisabeth P.

Published
2021
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3. Structural basis of the mechanism and inhibition of a human ceramide synthase

Author

Pascoa, Tomas C., primary, Pike, Ashley C.W., additional, Tautermann, Christofer S., additional, Chi, Gamma, additional, Traub, Michael, additional, Quigley, Andrew, additional, Chalk, Rod, additional, Štefanic, Saša, additional, Thamm, Sven, additional, Pautsch, Alexander, additional, Carpenter, Elisabeth P., additional, Schnapp, Gisela, additional, and Sauer, David B., additional

Published
2023
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5. High-Throughput Expression and Purification of Human Solute Carriers for Structural and Biochemical Studies

Author

Raturi, Sagar, primary, Li, Huanyu, additional, Chang, Yung-Ning, additional, Scacioc, Andreea, additional, Bohstedt, Tina, additional, Fernandez-Cid, Alejandra, additional, Evans, Adam, additional, Abrusci, Patrizia, additional, Balakrishnan, Abilasha, additional, Pascoa, Tomas C., additional, He, Didi, additional, Chi, Gamma, additional, Kaur Singh, Nanki, additional, Ye, Mingda, additional, Li, Anna, additional, Shrestha, Leela, additional, Wang, Dong, additional, Williams, Eleanor P., additional, Burgess-Brown, Nicola A., additional, Dürr, Katharina L., additional, Puetter, Vera, additional, Ingles-Prieto, Alvaro, additional, and Sauer, David B., additional

Published
2023
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6. The structural basis of fatty acid elongation by the ELOVL elongases

Author

Nie, Laiyin, primary, Pike, Ashley C. W., additional, Pascoa, Tomas C., additional, Bushell, Simon R., additional, Quigley, Andrew, additional, Ruda, Gian Filippo, additional, Chu, Amy, additional, Cole, Victoria, additional, Speedman, David, additional, Moreira, Tiago, additional, Shrestha, Leela, additional, Mukhopadhyay, Shubhashish M.M., additional, Burgess-Brown, Nicola A., additional, Love, James D., additional, Brennan, Paul E., additional, and Carpenter, Elisabeth P., additional

Published
2020
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7. Porphyrin-Assisted Docking of a Thermophage Portal Protein into Lipid Bilayers: Nanopore Engineering and Characterization

Author

Cressiot, Benjamin, primary, Greive, Sandra J., additional, Si, Wei, additional, Pascoa, Tomas C., additional, Mojtabavi, Mehrnaz, additional, Chechik, Maria, additional, Jenkins, Huw T., additional, Lu, Xueguang, additional, Zhang, Ke, additional, Aksimentiev, Aleksei, additional, Antson, Alfred A., additional, and Wanunu, Meni, additional

Published
2017
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8. Porphyrin-Assisted Docking of a Thermophage Portal Protein into Lipid Bilayers: Nanopore Engineering and Characterization

Author

Cressiot, Benjamin, Greive, Sandra J., Si, Wei, Pascoa, Tomas C., Mojtabavi, Mehrnaz, Chechik, Maria, Jenkins, Huw T., Lu, Xueguang, Zhang, Ke, Aksimentiev, Aleksei, Antson, Alfred A., and Wanunu, Meni

Abstract

Nanopore-based sensors for nucleic acid sequencing and single-molecule detection typically employ pore-forming membrane proteins with hydrophobic external surfaces, suitable for insertion into a lipid bilayer. In contrast, hydrophilic pore-containing molecules, such as DNA origami, have been shown to require chemical modification to favor insertion into a lipid environment. In this work, we describe a strategy for inserting polar proteins with an inner pore into lipid membranes, focusing here on a circular 12-subunit assembly of the thermophage G20c portal protein. X-ray crystallography, electron microscopy, molecular dynamics, and thermal/chaotrope denaturation experiments all find the G20c portal protein to have a highly stable structure, favorable for nanopore sensing applications. Porphyrin conjugation to a cysteine mutant in the protein facilitates the protein’s insertion into lipid bilayers, allowing us to probe ion transport through the pore. Finally, we probed the portal interior size and shape using a series of cyclodextrins of varying sizes, revealing asymmetric transport that possibly originates from the portal’s DNA-ratchet function.

Published
2024
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