3JUC

Human gamma-glutamylamine cyclotransferase complex with 5-oxoproline

3JUC の概要

• エントリーDOI: 10.2210/pdb3juc/pdb
• 関連するPDBエントリー: 3JUB 3JUD
• 分子名称: AIG2-like domain-containing protein 1, PYROGLUTAMIC ACID, NITRATE ION, ... (4 entities in total)
• 機能のキーワード: cyclotransferase, gamma-glutamylamine cyclotransferase, gamma-glutamyl-epsilon-lysine, epsilon-(gamma-glutamyl)-lysine, oxoproline, 5-oxo-l-proline, cyclotransferase fold, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17605.70

構造登録者

Oakley, A.J. (登録日: 2009-09-15, 公開日: 2010-02-09, 最終更新日: 2023-11-01)

主引用文献

Oakley, A.J.,Coggan, M.,Board, P.G.
Identification and characterization of {gamma}-glutamylamine cyclotransferase: An enzyme responsible for {gamma}-glutamyl-{epsilon}-lysine catabolism
J.Biol.Chem., 285:9642-9648, 2010

PubMed Abstract: Gamma-glutamylamine cyclotransferase (GGACT) is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline. GGACT shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. The enzyme adopts the newly identified cyclotransferase fold, observed in gamma-glutamylcyclotransferase (GGCT), an enzyme with activity toward gamma-glutamyl-alpha-amino acids (Oakley, A. J., Yamada, T., Liu, D., Coggan, M., Clark, A. G., and Board, P. G. (2008) J. Biol. Chem. 283, 22031-22042). Despite the absence of significant sequence identity, several residues are conserved in the active sites of GGCT and GGACT, including a putative catalytic acid/base residue (GGACT Glu(82)). The structure of GGACT in complex with the reaction product 5-oxoproline provides evidence for a common catalytic mechanism in both enzymes. The proposed mechanism, combined with the three-dimensional structures, also explains the different substrate specificities of these enzymes. Despite significant sequence divergence, there are at least three subfamilies in prokaryotes and eukaryotes that have conserved the GGCT fold and GGCT enzymatic activity.

PubMed: 20110353
DOI: 10.1074/jbc.M109.082099

実験手法

X-RAY DIFFRACTION (1.2 Å)