3JUD

Human gamma-glutamylamine cyclotransferase, E82Q mutant

Summary for 3JUD

• Entry DOI: 10.2210/pdb3jud/pdb
• Related: 3JUB 3JUC
• Descriptor: AIG2-like domain-containing protein 1, NITRATE ION (3 entities in total)
• Functional Keywords: cyclotransferase, gamma-glutamylamine cyclotransferase, gamma-glutamyl-epsilon-lysine, epsilon-(gamma-glutamyl)-lysine, oxoproline, 5-oxo-l-proline, cyclotransferase fold, mutant, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 17537.60

Authors

Oakley, A.J. (deposition date: 2009-09-15, release date: 2010-02-09, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (0.98 Å)