1pdh
From Proteopedia
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|PDB= 1pdh |SIZE=350|CAPTION= <scene name='initialview01'>1pdh</scene>, resolution 2.1Å | |PDB= 1pdh |SIZE=350|CAPTION= <scene name='initialview01'>1pdh</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAS:ARABINO-FLAVIN-ADENINE+DINUCLEOTIDE'>FAS</scene> | + | |LIGAND= <scene name='pdbligand=FAS:ARABINO-FLAVIN-ADENINE+DINUCLEOTIDE'>FAS</scene>, <scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/4-hydroxybenzoate_3-monooxygenase 4-hydroxybenzoate 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.2 1.14.13.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxybenzoate_3-monooxygenase 4-hydroxybenzoate 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.2 1.14.13.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pdh OCA], [http://www.ebi.ac.uk/pdbsum/1pdh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pdh RCSB]</span> | ||
}} | }} | ||
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[[Category: Eppink, M H.M.]] | [[Category: Eppink, M H.M.]] | ||
[[Category: Schreuder, H A.]] | [[Category: Schreuder, H A.]] | ||
| - | [[Category: FAS]] | ||
| - | [[Category: PHB]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:58:11 2008'' |
Revision as of 19:58, 30 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | , | ||||||
| Activity: | 4-hydroxybenzoate 3-monooxygenase, with EC number 1.14.13.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE RECONSTITUTED WITH THE MODIFIED FAD PRESENT IN ALCOHOL OXIDASE FROM METHYLOTROPHIC YEASTS: EVIDENCE FOR AN ARABINOFLAVIN
Overview
The flavin prosthetic group (FAD) of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens was replaced by a stereochemical analog, which is spontaneously formed from natural FAD in alcohol oxidases from methylotrophic yeasts. Reconstitution of p-hydroxybenzoate hydroxylase from apoprotein and modified FAD is a rapid process complete within seconds. Crystals of the enzyme-substrate complex of modified FAD-containing p-hydroxybenzoate hydroxylase diffract to 2.1 A resolution. The crystal structure provides direct evidence for the presence of an arabityl sugar chain in the modified form of FAD. The isoalloxazine ring of the arabinoflavin adenine dinucleotide (a-FAD) is located in a cleft outside the active site as recently observed in several other p-hydroxybenzoate hydroxylase complexes. Like the native enzyme, a-FAD-containing p-hydroxybenzoate hydroxylase preferentially binds the phenolate form of the substrate (pKo = 7.2). The substrate acts as an effector highly stimulating the rate of enzyme reduction by NADPH (kred > 500 s-1). The oxidative part of the catalytic cycle of a-FAD-containing p-hydroxybenzoate hydroxylase differs from native enzyme. Partial uncoupling of hydroxylation results in the formation of about 0.3 mol of 3,4-dihydroxybenzoate and 0.7 mol of hydrogen peroxide per mol NADPH oxidized. It is proposed that flavin motion in p-hydroxybenzoate hydroxylase is important for efficient reduction and that the flavin "out" conformation is associated with the oxidase activity.
About this Structure
1PDH is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
Reference
Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin., van Berkel WJ, Eppink MH, Schreuder HA, Protein Sci. 1994 Dec;3(12):2245-53. PMID:7756982
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