1JQP

dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family

Summary for 1JQP

• Entry DOI: 10.2210/pdb1jqp/pdb
• Descriptor: dipeptidyl peptidase I, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: cathepsin c, dpp i, papain, tetramer, chloride, cysteine protease, hydrolase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Lysosome: P80067
• Total number of polymer chains: 1
• Total formula weight: 50440.21

Authors

Olsen, J.G.,Kadziola, A.,Lauritzen, C.,Pedersen, J.,Larsen, S.,Dahl, S.W. (deposition date: 2001-08-08, release date: 2002-10-18, Last modification date: 2024-11-13)

Primary citation

Olsen, J.G.,Kadziola, A.,Lauritzen, C.,Pedersen, J.,Larsen, S.,Dahl, S.W.
Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain
FEBS LETT., 506:201-206, 2001

PubMed Abstract: 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 beta-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 12700 A3 spherical cavity. The tetramer contains six chloride ions, one buried in each S2 pocket and two at subunit interfaces.

PubMed: 11602245
DOI: 10.1016/S0014-5793(01)02911-8

Experimental method

X-RAY DIFFRACTION (2.4 Å)