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Journal articles
Secondary structure reshuffling modulates glycosyltransferase function at the membrane
David Giganti
1, 2
David Albesa-Jové
1, 3
Saioa Urresti
1, 3
Ane Rodrigo-Unzueta
1, 3
Mariano A Martínez
1
Natalia Comino
1, 3
Nathalie Barilone
2
Marco Bellinzoni
2
Alexandre Chenal
4
Marcelo E Guerin
5, 1, 3
Pedro M Alzari
2
David Giganti 1, 2
Author
David Albesa-Jové 1, 3
Author
Saioa Urresti 1, 3
Author
Ane Rodrigo-Unzueta 1, 3
Author
Mariano A Martínez 1
Author IdHAL : mariano-martinez ORCID : https://orcid.org/0000-0003-4460-8045
Natalia Comino 1, 3
Author
Nathalie Barilone 2
Author
Marco Bellinzoni 2
Author IdHAL : bellinzoni
1
Departamento de Bioquimica (48940 Leioa, Vizcaya - Spain)
- UPV/EHU - Universidad del Pais Vasco / Euskal Herriko Unibertsitatea [Espagne] (Barrio Sarriena s/n, 48940 Leioa, Bizkaia Campus d'Álava : Vice-Rectorado, San Antonio 41, 01005 Vitoria ; campus de Biscaye et services centraux : Apdo 1397, 48080 Bilbao ; campus de Guipúzcoa : Vice-Rectorado, Fuenterrabia 13-1° , 20006 San Sebastián - Spain)
2
Microb. Struc. (UMR_3528 / U-Pasteur_5) - Microbiologie structurale - Structural Microbiology (Département de Biologie structurale et Chimie, 25-28 rue du Dr Roux 75724 Paris cedex 15 - France)
- UPD7 - Université Paris Diderot - Paris 7 : UMR_3528 (5 rue Thomas-Mann - 75205 Paris cedex 13 - France)
- Institut Pasteur [Paris] : U-Pasteur_5 (25-28, rue du docteur Roux, 75724 Paris cedex 15 - France)
- CNRS - Centre National de la Recherche Scientifique : UMR_3528 (France)
3
Unidad de Biofísica (Barrio Sarriena s/n, Leioa, Bizkaia 48940 - Spain)
4
Biochimie des Interactions Macromoléculaires (Département de Biologie structurale et Chimie, 25-28 rue du Docteur Roux 75724 Paris cedex 15 - France)
- Institut Pasteur [Paris] (25-28, rue du docteur Roux, 75724 Paris cedex 15 - France)
- CNRS - Centre National de la Recherche Scientifique : UMR3528 (France)
Abstract : Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including β-strand-to-α-helix and α-helix-to-β-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane.
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Journal articles
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https://hal-pasteur.archives-ouvertes.fr/pasteur-01408804
Contributor : Bénédicte Benedic <>
Submitted on : Monday, December 5, 2016 - 2:05:11 PM
Last modification on : Thursday, June 11, 2020 - 12:00:05 PM
Long-term archiving on: : Monday, March 20, 2017 - 11:28:36 PM
Contributor : Bénédicte Benedic <>
Submitted on : Monday, December 5, 2016 - 2:05:11 PM
Last modification on : Thursday, June 11, 2020 - 12:00:05 PM
Long-term archiving on: : Monday, March 20, 2017 - 11:28:36 PM
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Identifiers
- HAL Id : pasteur-01408804, version 1
- DOI : 10.1038/nchembio.1694
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PASTEUR | CNRS | UNIV-PARIS7 | USPC | UNIV-PARIS | UP-SCIENCES
Citation
David Giganti, David Albesa-Jové, Saioa Urresti, Ane Rodrigo-Unzueta, Mariano A Martínez, et al.. Secondary structure reshuffling modulates glycosyltransferase function at the membrane. Nature Chemical Biology, Nature Publishing Group, 2014, 11 (1), pp.16 - 18. ⟨10.1038/nchembio.1694⟩. ⟨pasteur-01408804⟩
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