The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1

Autor: Graham C. Robinson, John V. Bason, Martin G. Montgomery, Ian M. Fearnley, David M. Mueller, Andrew G. W. Leslie, John E. Walker

Publikováno v: Open Biology, Vol 3, Iss 2 (2013)

The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by the yeast IF1 has been determined at 2.5 Å resolution. The inhibitory region of IF1 from residues 1 to 36 is entrapped between the C-terminal domains of the αDP- and βDP-subunit

Externí odkaz: https://doaj.org/article/786b3de32e564d7ca22815d4b8b27ec7

Crystal structure of the pseudoenzyme PDX1.2 in complex with its cognate enzyme PDX1.3: a total eclipse

Autor: Céline Roux, Teresa B. Fitzpatrick, Jacobo Martinez-Font, Stéphane Thore, Graham C Robinson, Markus Kaufmann, Michael Hothorn

Publikováno v: Acta Crystallographica. D, Biological Crystallography, Vol. 75, No Pt 4 (2019) pp. 400-415
Acta crystallographica. Section D, Structural biology
Acta crystallographica. Section D, Structural biology, International Union of Crystallography, 2019, 75 (4), pp.400-415. ⟨10.1107/S2059798319002912⟩

Pseudoenzymes have burst into the limelight recently as they provide another dimension to regulation of cellular protein activity. In the eudicot plant lineage, the pseudoenzyme PDX1.2 and its cognate enzyme PDX1.3 interact to regulate vitamin B6 bio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21d447ab2b595525acd7b5dd212a502a
https://archive-ouverte.unige.ch/unige:121408

Cloning, expression, purification, and characterisation of the HEAT-repeat domain of TOR from the thermophilic eukaryote Chaetomium thermophilum

Autor: Christl Gaubitz, Yogesh Vegunta, Graham C Robinson, Caroline Gabus, Stéphane Thore

Publikováno v: Protein Expression and Purification
Protein Expression and Purification, Elsevier, 2017, 133, pp.90-95. ⟨10.1016/j.pep.2017.03.007⟩

The Target of Rapamycin Complex is a central controller of cell growth and differentiation in eukaryotes. Its global architecture has been described by cryoelectron microscopy, and regions of its central TOR protein have been described by X-ray cryst

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1415e9dcddacee2986f494c161e43573
https://pubmed.ncbi.nlm.nih.gov/28284995

Molecular Basis of the Rapamycin Insensitivity of Target Of Rapamycin Complex 2

Autor: Alexander Leitner, Ruedi Aebersold, Delphine Rispal, Manikandan Karuppasamy, Taiana Maia de Oliveira, Robbie Loewith, Manoel Prouteau, Georgia Konstantinidou, Sandra Eltschinger, Christl Gaubitz, Christiane Schaffitzel, Graham C Robinson, Stéphane Thore

Publikováno v: Molecular Cell, Vol. 58, No 6 (2015) pp. 977-988
Molecular cell
Molecular Cell
Molecular Cell, Elsevier, 2015, 58 (6), pp.977-988. ⟨10.1016/j.molcel.2015.04.031⟩

Target of Rapamycin (TOR) plays central roles in the regulation of eukaryote growth as the hub of two essential multiprotein complexes: TORC1, which is rapamycin-sensitive, and the lesser characterized TORC2, which is not. TORC2 is a key regulator of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d87760e51f92036ecb84a672fe86648a
https://archive-ouverte.unige.ch/unige:103227

The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1

Autor: Martin G. Montgomery, John V. Bason, Andrew G. W. Leslie, Graham C Robinson, John E. Walker, David M. Mueller, Ian M. Fearnley

Publikováno v: Open Biology, Vol 3, Iss 2 (2013)
Open Biology

The structure of F 1 -ATPase from Saccharomyces cerevisiae inhibited by the yeast IF 1 has been determined at 2.5 Å resolution. The inhibitory region of IF 1 from residues 1 to 36 is entrapped between the C-terminal domains of the α DP - and β DP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eda0a5e68b7dfb6841fae14ac76496d6
https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.120164