3CSK

Structure of DPP III from Saccharomyces cerevisiae

3CSK の概要

• エントリーDOI: 10.2210/pdb3csk/pdb
• 分子名称: Probable dipeptidyl-peptidase 3, ZINC ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: zn-hydrolase, aminodipeptidase, hexxgh-motif, aminopeptidase, hydrolase, metal-binding, metalloprotease, protease
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Cytoplasm (Probable): Q08225
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 80763.21

構造登録者

Baral, P.K.,Jajcanin, N.,Deller, S.,Macheroux, P.,Abramic, M.,Gruber, K. (登録日: 2008-04-10, 公開日: 2008-06-10, 最終更新日: 2024-05-29)

主引用文献

Baral, P.K.,Jajcanin-Jozic, N.,Deller, S.,Macheroux, P.,Abramic, M.,Gruber, K.
The first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate binding.
J.Biol.Chem., 283:22316-22324, 2008

PubMed Abstract: Dipeptidyl-peptidases III (DPP III) are zinc-dependent enzymes that specifically cleave the first two amino acids from the N terminus of different length peptides. In mammals, DPP III is associated with important physiological functions and is a potential biomarker for certain types of cancer. Here, we present the 1.95-A crystal structure of yeast DPP III representing the prototype for the M49 family of metallopeptidases. It shows a novel fold with two domains forming a wide cleft containing the catalytic metal ion. DPP III exhibits no overall similarity to other metallopeptidases, such as thermolysin and neprilysin, but zinc coordination and catalytically important residues are structurally conserved. Substrate recognition is accomplished by a binding site for the N terminus of the peptide at an appropriate distance from the metal center and by a series of conserved arginine residues anchoring the C termini of different length substrates.

PubMed: 18550518
DOI: 10.1074/jbc.M803522200

実験手法

X-RAY DIFFRACTION (1.95 Å)