MDA5 disease variant M854K prevents ATP-dependent structural discrimination of viral and cellular RNA

Autor: Qin Yu, Yorgo Modis, Alba Herrero del Valle, Rahul Singh

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications, 12 (1)
Nature Communications

Our innate immune responses to viral RNA are vital defenses. Long cytosolic double-stranded RNA (dsRNA) is recognized by MDA5. The ATPase activity of MDA5 contributes to its dsRNA binding selectivity. Mutations that reduce RNA selectivity can cause a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7be0473d4f75a5612346c5478f88ed7f
https://doaj.org/article/4ed51115fdf7407f8d5ba6033a51c511

Catalytic trajectory of a dimeric nonribosomal peptide synthetase subunit with an inserted epimerase domain

Autor: Wang, Jialiang, Li, Dandan, Chen, Lu, Cao, Wei, Kong, Liangliang, Zhang, Wei, Croll, Tristan, Deng, Zixin, Liang, Jingdan, Wang, Zhijun

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Nature Communications

Nonribosomal peptide synthetases (NRPSs) are modular assembly-line megaenzymes that synthesize diverse metabolites with wide-ranging biological activities. The structural dynamics of synthetic elongation has remained unclear. Here, we present cryo-EM

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61e3e1850ca80afdf4d09f40052d7b23

Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD

Autor: David Ron, Luke A. Perera, Nathan R. Zaccai, Juliette M. Devos, Michael Haertlein, Steffen Preissler, Sylvain Prévost

Publikováno v: Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
'Nature Communications ', vol: 12, pages: 5004-1-5004-18 (2021)
Nature Communications

The endoplasmic reticulum (ER) Hsp70 chaperone BiP is regulated by AMPylation, a reversible inactivating post-translational modification. Both BiP AMPylation and deAMPylation are catalysed by a single ER-localised enzyme, FICD. Here we present crysta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33fec1d51daa416bb43bfc7f35f77745
https://www.repository.cam.ac.uk/handle/1810/325252

Structure of inhibitor-bound mammalian complex I

Autor: Ahmed-Noor A. Agip, Owen D. Jarman, Ville R. I. Kaila, Andrea Di Luca, Alexander Jussupow, Hannah R. Bridges, John J. Wright, Ana P. Gamiz-Hernandez, James N. Blaza, Maxie M. Roessler, Justin G. Fedor, Judy Hirst

Publikováno v: Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)

Respiratory complex I (NADH:ubiquinone oxidoreductase) captures the free energy from oxidising NADH and reducing ubiquinone to drive protons across the mitochondrial inner membrane and power oxidative phosphorylation. Recent cryo-EM analyses have pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d6065bd67490ffee2a777328029d2b0
https://www.repository.cam.ac.uk/handle/1810/311614

Structure of inhibitor-bound mammalian complex I

Autor: Bridges, Hannah R., Fedor, Justin G., Blaza, James N., Di Luca, Andrea, Jussupow, Alexander, Jarman, Owen D., Wright, John J., Agip, Ahmed-Noor A., Gamiz-Hernandez, Ana P., Roessler, Maxie M., Kaila, Ville R. I., Hirst, Judy

Funder: The Swedish National Infrastructure for Computing (SNIC, 2019/2-3) UK National Electron Bio-Imaging Centre (eBIC) at the Diamond Light Source, proposal EM16309, funded by the Wellcome Trust, MRC and BBSRC
Respiratory complex I (NADH:ubiq

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9a961e7f6d1de3cfb0fccaa25f03aefd