Characterization of a Glycyl-Specific TET Aminopeptidase Complex from Pyrococcus horikoshii
Author:
Affiliation:
1. Université Grenoble Alpes, CNRS, Commissariat à l'Énergie Atomique, Institut de Biologie Structurale, Grenoble, France
Abstract
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JB.00059-18
Reference39 articles.
1. Metalloaminopeptidases: Common Functional Themes in Disparate Structural Surroundings
2. Bacterial aminopeptidases: Properties and functions
3. TET peptidases: A family of tetrahedral complexes conserved in prokaryotes
4. Tetrahedral aminopeptidase: a novel large protease complex from archaea
5. Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation
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1. M42 aminopeptidase catalytic site: the structural and functional role of a strictly conserved aspartate residue;Proteins: Structure, Function, and Bioinformatics;2020-08-13
2. X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050;Journal of Visualized Experiments;2020-05-13
3. How metal cofactors drive dimer–dodecamer transition of the M42 aminopeptidase TmPep1050 of Thermotoga maritima;Journal of Biological Chemistry;2019-11
4. Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme;Emerging Topics in Life Sciences;2018-11-14
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