4S2T

Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: a cytosolic enzyme with a di-nuclear active site

4S2T の概要

• エントリーDOI: 10.2210/pdb4s2t/pdb
• 関連するPDBエントリー: 4S2R
• 関連するBIRD辞書のPRD_ID: PRD_000553
• 分子名称: Protein APP-1, apstatin, ZINC ION, ... (5 entities in total)
• 機能のキーワード: pitta-bread fold, metalloprotease, zinc binding, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Caenorhabditis elegans (roundworm)
• 細胞内の位置: Cytoplasm : O44750
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 146278.56

構造登録者

Iyer, S.,La-Borde, P.,Payne, K.A.P.,Parsons, M.R.,Turner, A.J.,Isaac, R.E.,Acharya, K.R. (登録日: 2015-01-22, 公開日: 2015-04-22, 最終更新日: 2024-04-03)

主引用文献

Iyer, S.,La-Borde, P.J.,Payne, K.A.,Parsons, M.R.,Turner, A.J.,Isaac, R.E.,Acharya, K.R.
Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site.
FEBS Open Bio, 5:292-302, 2015

PubMed Abstract: Eukaryotic aminopeptidase P1 (APP1), also known as X-prolyl aminopeptidase (XPNPEP1) in human tissues, is a cytosolic exopeptidase that preferentially removes amino acids from the N-terminus of peptides possessing a penultimate N-terminal proline residue. The enzyme has an important role in the catabolism of proline containing peptides since peptide bonds adjacent to the imino acid proline are resistant to cleavage by most peptidases. We show that recombinant and catalytically active Caenorhabditis elegans APP-1 is a dimer that uses dinuclear zinc at the active site and, for the first time, we provide structural information for a eukaryotic APP-1 in complex with the inhibitor, apstatin. Our analysis reveals that C. elegans APP-1 shares similar mode of substrate binding and a common catalytic mechanism with other known X-prolyl aminopeptidases.

PubMed: 25905034
DOI: 10.1016/j.fob.2015.03.013

実験手法

X-RAY DIFFRACTION (2.15 Å)