Concerted Structural Changes in the Peptidase and the Propeller Domains of Prolyl Oligopeptidase are Required for Substrate Binding

Prolyl oligopeptidase contains a peptidase domain and its catalytic triad is covered by the central tunnel of a seven-bladed β-propeller. This domain makes the enzyme an oligopeptidase by excluding large structured peptides from the active site. The apparently rigid crystal structure does not explai...

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Veröffentlicht in:	Journal of molecular biology 2004-07, Vol.340 (3), p.627-637
Hauptverfasser:	Szeltner, Zoltán, Rea, Dean, Juhász, Tünde, Renner, Veronika, Fülöp, Vilmos, Polgár, László
Format:	Artikel
Sprache:	eng
Schlagworte:	Catalysis disulfide bond formation Disulfides - chemistry Models, Molecular Peptide Hydrolases - chemistry Peptide Hydrolases - metabolism Protein Conformation protein stability Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism site-specific mutagenesis substrate binding Substrate Specificity
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