1al8
From Proteopedia
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| - | [[Image:1al8.gif|left|200px]] | + | [[Image:1al8.gif|left|200px]] |
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| - | '''THREE-DIMENSIONAL STRUCTURE OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS''' | + | {{Structure |
| + | |PDB= 1al8 |SIZE=350|CAPTION= <scene name='initialview01'>1al8</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> and <scene name='pdbligand=DHP:3-DECYL-2,5-DIOXO-4-HYDROXY-3-PYRROLINE'>DHP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/(S)-2-hydroxy-acid_oxidase (S)-2-hydroxy-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.15 1.1.3.15] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THREE-DIMENSIONAL STRUCTURE OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AL8 is a [ | + | 1AL8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AL8 OCA]. |
==Reference== | ==Reference== | ||
| - | Three-dimensional structures of glycolate oxidase with bound active-site inhibitors., Stenberg K, Lindqvist Y, Protein Sci. 1997 May;6(5):1009-15. PMID:[http:// | + | Three-dimensional structures of glycolate oxidase with bound active-site inhibitors., Stenberg K, Lindqvist Y, Protein Sci. 1997 May;6(5):1009-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9144771 9144771] |
[[Category: (S)-2-hydroxy-acid oxidase]] | [[Category: (S)-2-hydroxy-acid oxidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: inhibitor binding]] | [[Category: inhibitor binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:07 2008'' |
Revision as of 07:59, 20 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | (S)-2-hydroxy-acid oxidase, with EC number 1.1.3.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS
Overview
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.
About this Structure
1AL8 is a Single protein structure of sequence from Spinacia oleracea. Full crystallographic information is available from OCA.
Reference
Three-dimensional structures of glycolate oxidase with bound active-site inhibitors., Stenberg K, Lindqvist Y, Protein Sci. 1997 May;6(5):1009-15. PMID:9144771
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