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

Large oligomeric enzymes control a myriad of cellular processes, from protein synthesis and degradation to metabolism. The 0.5 MDa large TET2 aminopeptidase, a prototypical protease important for cellular homeostasis, degrades peptides within a ca. 60 Å wide tetrahedral chamber with four lateral op...

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Bibliographic Details
Main Authors:	Barducci, A. (Author), Bustamante, J.P (Author), Fraga, H. (Author), Gauto, D.F (Author), Hessel, A. (Author), Macek, P. (Author), Malinverni, D. (Author), Paloni, M. (Author), Schanda, P. (Author), Sučec, I. (Author)
Format:	Article
Language:	English
Published:	Nature Research 2022
Subjects:	aminopeptidase Aminopeptidases biodegradation catalysis catalyst cell component degradation enzyme enzyme activity homeostasis Magnetic Resonance Spectroscopy metabolism molecular dynamics Molecular Dynamics Simulation nuclear magnetic resonance nuclear magnetic resonance spectroscopy Nuclear Magnetic Resonance, Biomolecular peptide Peptides protein
Online Access:	View Fulltext in Publisher

by Barducci, A., Bustamante, J.P, Fraga, H., Gauto, D.F, Hessel, A., Macek, P., Malinverni, D., Paloni, M., Schanda, P., Sučec, I.
Published 2022

View Fulltext in Publisher

Article

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

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