1VZ3

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT

Summary for 1VZ3

• Entry DOI: 10.2210/pdb1vz3/pdb
• Related: 1E5T 1E8M 1E8N 1H2W 1H2X 1H2Y 1H2Z 1O6F 1O6G 1QFM 1QFS 1UOO 1UOP 1UOQ 1VZ2
• Descriptor: PROLYL ENDOPEPTIDASE, GLYCEROL (3 entities in total)
• Functional Keywords: hydrolase, prolyl oligopeptidase, amnesia, alpha/ beta-hydrolase, beta-propeller, serine protease
• Biological source: SUS SCROFA (PIG)
• Cellular location: Cytoplasm: P23687
• Total number of polymer chains: 1
• Total formula weight: 81326.85

Authors

Rea, D.,Fulop, V. (deposition date: 2004-05-14, release date: 2004-07-01, Last modification date: 2023-12-13)

Primary citation

Szeltner, Z.,Rea, D.,Juhasz, T.,Renner, V.,Fulop, V.,Polgar, L.
Concerted Structural Changes in the Peptidase and the Propeller Domains of Prolyl Oligopeptidase are Required for Substrate Binding
J.Mol.Biol., 340:627-, 2004

PubMed Abstract: Prolyl oligopeptidase contains a peptidase domain and its catalytic triad is covered by the central tunnel of a seven-bladed beta-propeller. This domain makes the enzyme an oligopeptidase by excluding large structured peptides from the active site. The apparently rigid crystal structure does not explain how the substrate can approach the catalytic groups. Two possibilities of substrate access were investigated: either blades 1 and 7 of the propeller domain move apart, or the peptidase and/or propeller domains move to create an entry site at the domain interface. Engineering disulfide bridges to the expected oscillating structures prevented such movements, which destroyed the catalytic activity and precluded substrate binding. This indicated that concerted movements of the propeller and the peptidase domains are essential for the enzyme action.

PubMed: 15210359
DOI: 10.1016/J.JMB.2004.05.011

Experimental method

X-RAY DIFFRACTION (1.6 Å)