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Akademický článek

Visualizing the transiently populated closed-state of human HSP90 ATP binding domain

Autor: Faustine Henot, Elisa Rioual, Adrien Favier, Pavel Macek, Elodie Crublet, Pierre Josso, Bernhard Brutscher, Matthias Frech, Pierre Gans, Claire Loison, Jerome Boisbouvier

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

To refold client proteins, HSP90 chaperone undergoes large structural rearrangements. Here the authors use NMR and molecular simulation and reveal structure and dynamics of a key functionally relevant metastable state of human HSP90α N-terminal doma

Externí odkaz: https://doaj.org/article/a0e415192adb4a8f825b0f4fa98dd24f

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Akademický článek

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

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Akademický článek

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

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Akademický článek

Publisher Correction: 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 1-1 (2022)

Externí odkaz: https://doaj.org/article/b700f5fa44c44071a611f4bfd200650f

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Akademický článek

Structural Basis of Ca2+-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins

Autor: Vojtech Kuban, Pavel Macek, Jozef Hritz, Katerina Nechvatalova, Katerina Nedbalcova, Martin Faldyna, Peter Sebo, Lukas Zidek, Ladislav Bumba

Publikováno v: mBio, Vol 11, Iss 2 (2020)

ABSTRACT The posttranslational Ca2+-dependent “clip-and-link” activity of large repeat-in-toxin (RTX) proteins starts by Ca2+-dependent structural rearrangement of a highly conserved self-processing module (SPM). Subsequently, an internal asparta

Externí odkaz: https://doaj.org/article/fdc4a6e79d8040c09e2fbb26185124d6

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Backbone and methyl resonances assignment of the 87 kDa prefoldin from Pyrococcus horikoshii

Autor: Pierre Gans, Faustine Henot, Rida Awad, Pavel Macek, Jérôme Boisbouvier, Ricarda Törner

Publikováno v: Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2021, ⟨10.1007/s12104-021-10029-4⟩
Biomolecular NMR Assignments, 2021, ⟨10.1007/s12104-021-10029-4⟩

International audience; Prefoldin is a heterohexameric protein assembly which acts as a co-chaperonin for the well conserved Hsp60 chaperonin, present in archaebacteria and the eukaryotic cell cytosol. Prefoldin is a holdase, capturing client protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9b12e25cd6fc14d655b4811f18cdc14
https://doi.org/10.1007/s12104-021-10029-4

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Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 kDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle Spinning NMR

Autor: Diego F. Gauto, David Gajan, Roman J. Lichtenecker, Alessandro Barducci, Audrey Hessel, Masatsune Kainosho, Paul Schanda, Pavel Macek, Yohei Miyanoiri, Tsutomu Terauchi, Jérôme Boisbouvier, Hugo Pacheco de Freitas Fraga

Publikováno v: Journal of the American Chemical Society. 141:11183-11195

Aromatic residues are located at structurally important sites of many proteins. Probing their interactions and dynamics can provide important functional insight but is challenging in large proteins. Here, we introduce approaches to characterize the d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::243468560f6302c0b2934a75135d56b1
https://doi.org/10.1021/jacs.9b04219

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Optimized precursor to simplify assignment transfer between backbone resonances and stereospecifically labelled valine and leucine methyl groups: application to human Hsp90 N-terminal domain

Autor: Elodie Crublet, Rime Kerfah, Ricarda Törner, Matthias Frech, Faustine Henot, Pierre Gans, Pavel Macek, Olivier Hamelin, Jérôme Boisbouvier

Publikováno v: Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2021, 75 (6-7), pp.221-232. ⟨10.1007/s10858-021-00370-0⟩
Journal of Biomolecular NMR, 2021, 75 (6-7), pp.221-232. ⟨10.1007/s10858-021-00370-0⟩

International audience; Methyl moieties are highly valuable probes for quantitative NMR studies of large proteins. Hence, their assignment is of the utmost interest to obtain information on both interactions and dynamics of proteins in solution. Here

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71d1d542d336b263508f1ea2d5f8d0f8
https://pubmed.ncbi.nlm.nih.gov/34041691

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Structural Basis of Ca2+-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins

Autor: Martin Faldyna, Vojtech Kuban, Lukas Zidek, Katerina Nedbalcova, Peter Sebo, Ladislav Bumba, Jozef Hritz, Pavel Macek, Katerina Nechvatalova

Publikováno v: mBio, Vol 11, Iss 2 (2020)
mBio
mBio, Vol 11, Iss 2, p e00226-20 (2020)

The Ca2+-dependent clip-and-link activity of large repeat-in-toxin (RTX) proteins is an exceptional posttranslational process in which an internal domain called a self-processing module (SPM) mediates Ca2+-dependent processing of a highly specific as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d1ba3aa675f1e2de4b29d8ad5b54181
https://journals.asm.org/doi/10.1128/mBio.00226-20

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Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration

Autor: Pavel Macek, Jonathan P. Waltho, J. Willem M. Nissink, Matthew J. Cliff, Kevin J. Embrey, Rick Davies, Martin Blackledge, Stanislava Panova, Malene Ringkjøbing Jensen

Publikováno v: Structure
Structure, Elsevier (Cell Press), 2019, 27 (10), pp.1537-1546.e4. ⟨10.1016/j.str.2019.07.006⟩
Panova, S, Cliff, M, Macek, P, Blackledge, M, Jensen, M R, Nissink, J W M, Embrey, K J, Davies, R & Waltho, J 2019, ' Mapping hidden residual structure within the Myc bHLH-LZ domain using chemical denaturant titration ', Structure . https://doi.org/10.1016/j.str.2019.07.006
Structure, 2019, 27 (10), pp.1537-1546.e4. ⟨10.1016/j.str.2019.07.006⟩

International audience; Intrinsically disordered proteins (IDPs) underpin biological regulation and hence are highly desirable drug-development targets. NMR is normally the tool of choice for studying the conformational preferences of IDPs, but the a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2279504f4c486d035e0b61eb94e5db50
https://hal.univ-grenoble-alpes.fr/hal-03016176/document

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