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PDBsum entry 2d33
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References listed in PDB file
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Key reference
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Title
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Structural basis of efficient coupling between peptide ligation and ATP hydrolysis by gamma-Gluatamylcysteine synthetase
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Authors
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T.Hibi,
M.Nakayama,
H.Nii,
Y.Kurokawa,
H.Katano,
J.Oda.
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Ref.
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To be Published ...
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Secondary reference #1
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Title
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Crystal structure of gamma-Glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis.
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Authors
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T.Hibi,
H.Nii,
T.Nakatsu,
A.Kimura,
H.Kato,
J.Hiratake,
J.Oda.
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Ref.
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Proc Natl Acad Sci U S A, 2004,
101,
15052-15057.
[DOI no: ]
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PubMed id
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Figure 3.
Fig. 3. Stereoview of the residues surrounding the
Cys-analog moiety of sulfoximine 2, showing the distances
between the ligands. The molecular surface around the
Cys-binding site is drawn in white.
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Figure 5.
Fig. 5. Superimposition of residues 238-251, including the
switch loop. The loop's hinge residues, Gly-240 and Leu-249, are
labeled.
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Secondary reference #2
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Title
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Escherichia coli b gamma-Glutamylcysteine synthetase: modification, Purification, Crystallization and preliminary crystallographic analysis.
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Authors
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T.Hibi,
H.Hisada,
T.Nakatsu,
H.Kato,
J.Oda.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2002,
58,
316-318.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2 The self-rotation function of  GCS
at  angles
of (a) 180° and (b) 120°. The data are in the resolution range
10.0-3.0 Å and the integration radius is 30.0 Å.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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