5DZU

Structure of potato cathepsin D inhibitor

Summary for 5DZU

• Entry DOI: 10.2210/pdb5dzu/pdb
• Descriptor: Aspartic protease inhibitor 11, GLYCEROL, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: kunitz-type protease inhibitor, hydrolase inhibitor
• Biological source: Solanum tuberosum (Potato)
• Cellular location: Vacuole : P16348
• Total number of polymer chains: 2
• Total formula weight: 41680.60

Authors

Guo, J.,Erskine, P.,Coker, A.R.,Wood, S.P.,Cooper, J.B. (deposition date: 2015-09-26, release date: 2015-10-21, Last modification date: 2024-10-16)

Primary citation

Guo, J.,Erskine, P.T.,Coker, A.R.,Wood, S.P.,Cooper, J.B.
Structure of a Kunitz-type potato cathepsin D inhibitor.
J.Struct.Biol., 192:554-560, 2015

PubMed Abstract: Potato cathepsin D inhibitor (PDI) is a glycoprotein of 188 amino acids which can inhibit both the aspartic protease cathepsin D and the serine protease trypsin. Here we report the first X-ray structure of PDI at a resolution of 2.1 Å showing that PDI adopts a β-trefoil fold, which is typical of the Kunitz-family protease inhibitors, with the inhibitory loops protruding from the core. Possible reactive-site loops including one involving a unique disulphide and another involving a protruding 310 helix are identified and docking studies indicate the mode of action of this unusual bi-functional inhibitor.

PubMed: 26542926
DOI: 10.1016/j.jsb.2015.10.020

Experimental method

X-RAY DIFFRACTION (2.12 Å)