Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR

Autor: Diego F. Gauto, Pavel Macek, Duccio Malinverni, Hugo Fraga, Matteo Paloni, Iva Sučec, Audrey Hessel, Juan Pablo Bustamante, Alessandro Barducci, Paul Schanda

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

Motion is key to enzymatic catalysis. Gauto et al. show that a flexible loop region is crucial for the function of an aminopeptidase and show that magic-angle spinning NMR provides atomic-level quantitative insights in this very large complex.

Externí odkaz: https://doaj.org/article/ab237d89762e45b3a86e9647c96705ee

Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex

Autor: Diego F. Gauto, Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin, Pavel Macek, Remy Sounier, Astrid C. Sivertsen, Elena Schmidt, Rime Kerfah, Guillaume Mas, Jacques-Philippe Colletier, Peter Güntert, Adrien Favier, Guy Schoehn, Paul Schanda, Jerome Boisbouvier

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)

NMR structure determination is challenging for proteins with a molecular weight above 30 kDa and atomic-resolution structure determination from cryo-EM data is currently not the rule. Here the authors describe an integrated structure determination ap

Externí odkaz: https://doaj.org/article/b46e113a51c845d98317d17073be2ebe

Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD

Autor: Diego F. Gauto, Olga O. Lebedenko, Lea Marie Becker, Isabel Ayala, Roman Lichtenecker, Nikolai R. Skrynnikov, Paul Schanda

Publikováno v: Journal of structural biology: X. 7

Probing the dynamics of aromatic side chains provides important insights into the behavior of a protein because flips of aromatic rings in a protein’s hydrophobic core report on breathing motion involving a large part of the protein. Inherently inv

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21fa50d8eeeb1ee9ab23bfb40c615210
https://pubmed.ncbi.nlm.nih.gov/36578472

The key role of electrostatic interactions in the induced folding in RNA recognition by DCL1-A

Autor: Jin Wang, Irina P. Suarez, Diego F. Gauto, Lingci Zhao, Rodolfo M. Rasia

Publikováno v: CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET

The intrinsically disordered protein domain DCL1-A is the first report of a complete double stranded RNA binding domain folding upon binding. DCL1-A recognizes the dsRNA by acquiring a well-folded structure after engagement with its interaction partn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::822db709c5c8ff6a249fded5b5f1a83d
https://doi.org/10.1039/c7cp07889g

Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors

Autor: Audrey Hessel, Katharina Weinhäupl, Adrián Velázquez-Campoy, Christophe Chipot, Cécile Morlot, Paul Schanda, Jan Felix, François Dehez, Olga Abian, Hugo Pacheco de Freitas Fraga, Irina Gutsche, Diego F. Gauto

Publikováno v: Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname
'Science Advances ', vol: 5, pages: eaaw3818-1-eaaw3818-19 (2019)
Science Advances
Science Advances, American Association for the Advancement of Science (AAAS), 2019, 5 (9), pp.eaaw3818. ⟨10.1126/sciadv.aaw3818⟩
SCIENCE ADVANCES
Digital.CSIC. Repositorio Institucional del CSIC
Science Advances, 2019, 5 (9), pp.eaaw3818. ⟨10.1126/sciadv.aaw3818⟩

18 pags., 6 figs., 1 tab. -- Open Access funded by Creative Commons Atribution Licence 4.0
Coordinated conformational transitions in oligomeric enzymatic complexes modulate function in response to substrates and play a crucial role in enzyme inh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a1324138b0f4d564dc88daa4ccd2c80