15N relaxation NMR studies of prolyl oligopeptidase, an 80 kDa enzyme, reveal a pre-existing equilibrium between different conformational states

Nessim Kichik; Teresa Tarragó; Birgit Claasen; Margarida Gairí; Oscar Millet; Ernest Giralt

doi:10.1002/cbic.201100614

15N relaxation NMR studies of prolyl oligopeptidase, an 80 kDa enzyme, reveal a pre-existing equilibrium between different conformational states

Chembiochem. 2011 Dec 16;12(18):2737-9. doi: 10.1002/cbic.201100614. Epub 2011 Nov 8.

Authors

Nessim Kichik¹, Teresa Tarragó, Birgit Claasen, Margarida Gairí, Oscar Millet, Ernest Giralt

Affiliation

¹ Institute for Research in Biomedicine, Baldiri Reixac 10, 08028 Barcelona, Spain.

PMID: 22069228
DOI: 10.1002/cbic.201100614

Abstract

Open and closed: The characterization of protein mobility is crucial for the understanding of biological functions. We have applied NMR spectroscopy to study the conformational dynamics of the 80 kDa enzyme prolyl oligopeptidase (POP). Our results revealed that POP is highly dynamic and that inhibition of catalytic activity shifts this conformational equilibrium towards a less dynamic state.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Models, Molecular
Nitrogen Isotopes*
Nuclear Magnetic Resonance, Biomolecular
Prolyl Oligopeptidases
Protein Conformation
Serine Endopeptidases / chemistry*
Swine

Substances

Nitrogen Isotopes
Serine Endopeptidases
Prolyl Oligopeptidases