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PDBsum entry 1al8
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References listed in PDB file
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Key reference
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Title
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Three-Dimensional structures of glycolate oxidase with bound active-Site inhibitors.
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Authors
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K.Stenberg,
Y.Lindqvist.
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Ref.
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Protein Sci, 1997,
6,
1009-1015.
[DOI no: ]
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PubMed id
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Abstract
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A key step in plant photorespiration, the oxidation of glycolate to glyoxylate,
is carried out by the peroxisomal flavoprotein glycolate oxidase (EC 1.1.3.15).
The three-dimensional structure of this alpha/beta barrel protein has been
refined to 2 A resolution (Lindqvist Y. 1989. J Mol Biol 209:151-166). FMN
dependent glycolate oxidase is a member of the family of alpha-hydroxy acid
oxidases. Here we describe the crystallization and structure determination of
two inhibitor complexes of the enzyme, TKP
(3-Decyl-2,5-dioxo-4-hydroxy-3-pyrroline) and TACA
(4-Carboxy-5-(1-pentyl)hexylsulfanyl-1,2,3-triazole). The structure of the TACA
complex has been refined to 2.6 A resolution and the TKP complex, solved with
molecular replacement, to 2.2 A resolution. The Rfree for the TACA and TKP
complexes are 24.2 and 25.1%, respectively. The overall structures are very
similar to the unliganded holoenzyme, but a closer examination of the active
site reveals differences in the positioning of the flavin isoalloxazine ring and
a displaced flexible loop in the TKP complex. The two inhibitors differ in
binding mode and hydrophobic interactions, and these differences are reflected
by the very different Ki values for the inhibitors, 16 nM for TACA and 4.8
microM for TKP. Implications of the structures of these enzyme-inhibitor
complexes for the model for substrate binding and catalysis proposed from the
holo-enzyme structure are discussed.
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Secondary reference #1
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Title
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High-Level expression, Purification, And crystallization of recombinant spinach glycolate oxidase in escherichia coli.
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Authors
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K.Stenberg,
Y.Lindqvist.
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Ref.
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Protein Expr Purif, 1996,
8,
295-298.
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PubMed id
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Secondary reference #2
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Title
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Refined structure of spinach glycolate oxidase at 2 a resolution.
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Author
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Y.Lindqvist.
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Ref.
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J Mol Biol, 1989,
209,
151-166.
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PubMed id
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