Müller, Jonathan W.; Link, Nina C; Matena, Anja; Hoppstock, Lukas; Rüppel, Alma; Bayer, Peter; Blankenfeldt, Wulf:
Crystallographic Proof for an Extended Hydrogen Bonding Network in Small Prolyl Isomerases
2011
In: Journal of the American Chemical Society, Jg. 133 (2011), Heft 50, S. 20096 - 20099
Artikel/Aufsatz in Zeitschrift / Fach: Biologie
Fakultät für Biologie » Chemische Biologie
Titel:
Crystallographic Proof for an Extended Hydrogen Bonding Network in Small Prolyl Isomerases
Autor(in):
Müller, Jonathan W. im Online-Personal- und -Vorlesungsverzeichnis LSF anzeigen; Link, Nina C; Matena, Anja im Online-Personal- und -Vorlesungsverzeichnis LSF anzeigen; Hoppstock, Lukas; Rüppel, Alma im Online-Personal- und -Vorlesungsverzeichnis LSF anzeigen; Bayer, Peter im Online-Personal- und -Vorlesungsverzeichnis LSF anzeigen; Blankenfeldt, Wulf
Erscheinungsjahr
2011
Erschienen in:
Journal of the American Chemical Society, Jg. 133 (2011), Heft 50, S. 20096 - 20099
DOI
Signatur der UB
WWW URL

Abstract:

Parvulins compose a family of small peptidylprolyl isomerases (PPIases) involved in protein folding and protein quality control. A number of amino acids in the catalytic cavity are highly conserved, but their precise role within the catalytic mechanismis unknown. The 0.8 Å crystal structure of the prolyl isomerase domain of parvulin Par14 shows the electron density of hydrogen atoms between the D74, H42, H123, and T118 side chains. This threonine residue has previously not been associated with catalysis, but a corresponding T152A mutant of Pin1 shows a dramatic reduction of catalytic activity without compromising protein stability. The observed catalytic tetrad is strikingly conserved in Pin1- and parvulin-type proteins and hence constitutes a common feature of small peptidyl prolyl isomerases.