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Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro‐part domain
Author(s) -
Olsen Johan Gotthardt,
Kadziola Anders,
Lauritzen Conni,
Pedersen John,
Larsen Sine,
Dahl Søren Weis
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02911-8
Subject(s) - tetramer , papain , chemistry , dipeptidyl peptidase , substrate (aquarium) , protein subunit , carboxylate , cathepsin c , stereochemistry , protein structure , crystallography , enzyme , biophysics , biochemistry , biology , proteases , ecology , gene
The crystal structure of mature dipeptidyl peptidase I reveals insight into the unique tetrameric structure, substrate binding and activation of this atypical papain family peptidase. Each subunit is composed of three peptides. The heavy and light chains form the catalytic domain, which adopts the papain fold. The residual pro‐part forms a β‐barrel with the carboxylate group of Asp1 pointing towards the substrate amino‐terminus. The tetrameric structure appears to stabilize the association of the two domains and encloses a 12 700 Å 3 spherical cavity. The tetramer contains six chloride ions, one buried in each S2 pocket and two at subunit interfaces.