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

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

Show other versions (1)

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...

Full description

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

Internet

View Fulltext in Publisher

Similar Items