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Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant
Descriptor:	Gamma-glutamyltranspeptidase, S-(P-NITROBENZYL)GLUTATHIONE
Authors:	Barycki, J.J, Boanca, G, Sand, A.
Deposit date:	2007-07-15
Release date:	2008-02-12
Last modified:	2023-08-30
Method:	X-RAY DIFFRACTION (1.55 Å)
Cite:	Characterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis. Biochemistry, 46, 2007

Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase in Complex with Glutamate
Descriptor:	GLUTAMIC ACID, Gamma-glutamyltranspeptidase
Authors:	Barycki, J.J, Sand, A, Boanca, G.
Deposit date:	2007-07-14
Release date:	2008-02-12
Last modified:	2023-08-30
Method:	X-RAY DIFFRACTION (1.6 Å)
Cite:	Characterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis. Biochemistry, 46, 2007

Crystal Structure of Helicobacter pylori gamma-Glutamyltranspeptidase
Descriptor:	Gamma-glutamyltranspeptidase
Authors:	Boanca, G, Sand, A, Okada, T, Suzuki, H, Kumagai, H, Fukuyama, K, Barycki, J.J.
Deposit date:	2006-10-31
Release date:	2006-11-21
Last modified:	2023-08-30
Method:	X-RAY DIFFRACTION (1.9 Å)
Cite:	Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad. J.Biol.Chem., 282, 2007

Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis
Descriptor:	(2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC ACID, Gamma-glutamyltranspeptidase (Ggt) Large subunit, Gamma-glutamyltranspeptidase (Ggt) Small subunit
Authors:	Williams, K, Cullati, S, Sand, A, Biterova, E.I, Barycki, J.J.
Deposit date:	2008-12-25
Release date:	2009-05-19
Last modified:	2017-11-01
Method:	X-RAY DIFFRACTION (1.7 Å)
Cite:	Crystal Structure of Acivicin-Inhibited gamma-Glutamyltranspeptidase Reveals Critical Roles for Its C-Terminus in Autoprocessing and Catalysis. Biochemistry, 48, 2009