 |
PDBsum entry 1glv
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Glutathione biosynthesis ligase
|
PDB id
|
|
|
|
1glv
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Three-Dimensional structure of the glutathione synthetase from escherichia coli b at 2.0 a resolution.
|
|
|
Authors
|
|
H.Yamaguchi,
H.Kato,
Y.Hata,
T.Nishioka,
A.Kimura,
J.Oda,
Y.Katsube.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
229,
1083-1100.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Glutathione synthetase (gamma-L-glutamyl-L-cysteine: glycine ligase
(ADP-forming) EC 6.3.2.3: GSHase) catalyzes the synthesis of glutathione from
gamma-L-glutamyl-L-cysteine and Gly in the presence of ATP. The enzyme from
Escherichia coli is a tetramer with four identical subunits of 316 amino acid
residues. The crystal structure of the enzyme has been determined by isomorphous
replacement and refined to a 2.0 A resolution. Two regions, Gly164 to Gly167 and
Ile226 to Arg241, are invisible on the electron density map. The refined model
of the subunit includes 296 amino acid residues and 107 solvent molecules. The
crystallographic R-factor is 18.6% for 17.914 reflections with F > 3 sigma
between 6.0 A and 2.0 A. The structure consists of three domains: the
N-terminal, central, and C-terminal domains. In the tetrameric molecule, two
subunits that are in close contact form a tight dimer, two tight dimers forming
a tetramer with two solvent regions. The ATP molecule is located in the cleft
between the central and C-terminal domains. The ATP binding site is surrounded
by two sets of the structural motif that belong to those respective domains.
Each motif consists of an anti-parallel beta-sheet and a glycine-rich loop.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystallization and preliminary X-Ray studies of glutathione synthetase from escherichia coli b.
|
|
|
Authors
|
|
H.Kato,
H.Yamaguchi,
Y.Hata,
T.Nishioka,
Y.Katsube,
J.Oda.
|
|
|
Ref.
|
|
J Mol Biol, 1989,
209,
503-504.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Overexpression of glutathione synthetase in escherichia coli
|
|
|
Authors
|
|
H.Kato,
M.Kobayashi,
K.Murata,
T.Nishioka,
J.Oda.
|
|
|
Ref.
|
|
agric biol chem, 1989,
53,
3071.
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
Role of cysteine residues in glutathione synthetase from escherichia coli b. Chemical modification and oligonucleotide site-Directed mutagenesis.
|
|
|
Authors
|
|
H.Kato,
T.Tanaka,
T.Nishioka,
A.Kimura,
J.Oda.
|
|
|
Ref.
|
|
J Biol Chem, 1988,
263,
11646-11651.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
