In vitro evolution predicts emerging SARS-CoV-2 mutations with high affinity for ACE2 and cross-species binding.

Autor: Neil Bate, Christos G Savva, Peter C E Moody, Edward A Brown, Sian E Evans, Jonathan K Ball, John W R Schwabe, Julian E Sale, Nicholas P J Brindle

Publikováno v: PLoS Pathogens, Vol 18, Iss 7, p e1010733 (2022)

Emerging SARS-CoV-2 variants are creating major challenges in the ongoing COVID-19 pandemic. Being able to predict mutations that could arise in SARS-CoV-2 leading to increased transmissibility or immune evasion would be extremely valuable in develop

Externí odkaz: https://doaj.org/article/1c450b5c20754a42910056edeab3abf1

Binding of l-kynurenine to X. campestris tryptophan 2,3-dioxygenase

Autor: Mehul H. Jesani, Jonathan Clayden, Laura P. Campbell, Sarah J. Thackray, Jaswir Basran, Peter C. E. Moody, Emma Lloyd Raven, Elizabeth S. Booth, Christopher G. Mowat, Hanna Kwon

Publikováno v: Basran, J, Booth, E S, Campbell, L P, Thackray, S J, Jesani, M H, Clayden, J, Moody, P C E, Mowat, C G, Kwon, H & Raven, E L 2021, ' Binding of L-kynurenine to X. campestris tryptophan 2,3-dioxygenase ', Journal of Inorganic Biochemistry, vol. 225, 111604 . https://doi.org/10.1016/j.jinorgbio.2021.111604

The kynurenine pathway is the major route of tryptophan metabolism. The first step of this pathway is catalysed by one of two heme-dependent dioxygenase enzymes – tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) – leading in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c9ed062898cb8f82251351b97a81a35
https://pubmed.ncbi.nlm.nih.gov/34571402

Visualizing the protons in a metalloenzyme electron proton transfer pathway

Autor: Tobias E. Schrader, Reynier Suardíaz, Marc W. van der Kamp, Matthew P. Blakeley, Andreas Ostermann, Jaswir Basran, Hanna Kwon, Adrian J. Mulholland, Juliette M. Devos, Emma Lloyd Raven, Peter C. E. Moody

Publikováno v: Kwon, H, Basran, J, Devos, J M, Suardiaz Del Rio, R, Van Der Kamp, M W, Mulholland, A J, Schrader, T E, Ostermann, A, Blakeley, M P, Moody, P C E & Raven, E 2020, ' Visualizing the protons in a metalloenzyme electron proton transfer pathway ', Proceedings of the National Academy of Sciences of the United States of America . https://doi.org/10.1073/pnas.1918936117
Proceedings of the National Academy of Sciences of the United States of America 117(12), 6484-6490 (2020). doi:10.1073/pnas.1918936117
Proc Natl Acad Sci U S A

In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including resp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d5d0c60b8dad118e90a1a4953bb4391
https://research-information.bris.ac.uk/en/publications/1fb08f30-b3f4-4c9c-8b9c-70b658dc8784

Heme peroxidase—Trapping intermediates by cryo neutron crystallography

Autor: Hanna, Kwon, Tobias E, Schrader, Andreas, Ostermann, Matthew P, Blakeley, Emma L, Raven, Peter C E, Moody

Publikováno v: Methods in enzymology 634, 379-389 (2020). doi:10.1016/bs.mie.2020.01.010

By combining the normal practice for X-ray crystallography of collecting diffraction data at 100K with neutron crystallography the structures of cryo-trapped enzyme intermediates have been determined, revealing the positions of the previously hidden

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::235d6c3b5faa97c58464b95faa734c5e
https://hdl.handle.net/2128/30474

Heme peroxidase—Trapping intermediates by cryo neutron crystallography

Autor: Andreas Ostermann, Hanna Kwon, Tobias E. Schrader, Peter C. E. Moody, Emma Lloyd Raven, Matthew P. Blakeley

By combining the normal practice for X-ray crystallography of collecting diffraction data at 100 K with neutron crystallography the structures of cryo-trapped enzyme intermediates have been determined, revealing the positions of the previously hidden

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::414c2b01017c39f04debd8e10843e8f4
https://doi.org/10.1016/bs.mie.2020.01.010