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PDBsum entry 1gc2
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the pyridoxal 5'-Phosphate dependent l-Methionine gamma-Lyase from pseudomonas putida.
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Authors
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H.Motoshima,
K.Inagaki,
T.Kumasaka,
M.Furuichi,
H.Inoue,
T.Tamura,
N.Esaki,
K.Soda,
N.Tanaka,
M.Yamamoto,
H.Tanaka.
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Ref.
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J Biochem (tokyo), 2000,
128,
349-354.
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PubMed id
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Abstract
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L-Methionine gamma-lyase (MGL) catalyzes the pyridoxal 5'-phosphate (PLP)
dependent alpha,gamma-elimination of L-methionine. We have determined two
crystal structures of MGL from Pseudomonas putida using MAD (multiwavelength
anomalous diffraction) and molecular replacement methods. The structures have
been refined to an R-factor of 21.1% at 2.0 and 1.7 A resolution using
synchrotron radiation diffraction data. A homotetramer with 222 symmetry is
built up by non-crystallographic symmetry. Two monomers associate to build the
active dimer. The spatial fold of subunits, with three functionally distinct
domains and their quarternary arrangement, is similar to those of
L-cystathionine beta-lyase and L-cystathionine gamma-synthase from Escherichia
coli.
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Secondary reference #1
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Title
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Structural analysis of the l-Methionine gamma-Lyase gene from pseudomonas putida.
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Authors
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H.Inoue,
K.Inagaki,
M.Sugimoto,
N.Esaki,
K.Soda,
H.Tanaka.
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Ref.
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J Biochem (tokyo), 1995,
117,
1120-1125.
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PubMed id
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Secondary reference #2
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Title
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Crystal structure of the pyridoxal-5'-Phosphate dependent cystathionine beta-Lyase from escherichia coli at 1.83 a.
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Authors
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T.Clausen,
R.Huber,
B.Laber,
H.D.Pohlenz,
A.Messerschmidt.
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Ref.
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J Mol Biol, 1996,
262,
202-224.
[DOI no: ]
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PubMed id
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Figure 11.
Figure 11. Proposed reaction mechanism (A)--(F) for inactivation of CBL by F3Ala. Lys210 is the nucleophile at the
active site that reacts via Michael addition with the so-called activated Michael acceptor (C). Subsequent elimination
of HF from C
b
results in the inactivation end product (F) which was observed in the crystal structure of the CBL--F3Ala
complex. Abbreviation used: Pyr-C = NH
+
, enzyme-bound PLP.
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Figure 13.
Figure 13. Proposed reaction
mechanism for CBL. The colors
used are: apoprotein, red; cofactor,
black; substrate, blue. (a) Residues
involved in substrate binding. (b)
Residues essential for catalysis. (c)
Mechanism of C
b
-S bond cleavage
(Pyr-C = NH
+
, PLP derivative).
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #3
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Title
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Crystal structure of escherichia coli cystathionine gamma-Synthase at 1.5 a resolution.
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Authors
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T.Clausen,
R.Huber,
L.Prade,
M.C.Wahl,
A.Messerschmidt.
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Ref.
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Embo J, 1998,
17,
6827-6838.
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PubMed id
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