3pcj
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STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 2-HYDROXYISONICOTINIC ACID N-OXIDE
OverviewOverview
Protocatechuate 3,4-dioxygenase (3,4-PCD) utilizes a ferric ion to, catalyze the aromatic ring cleavage of 3,4-dihydroxybenzoate (PCA) by, incorporation of both atoms of dioxygen to yield beta-carboxy-cis, cis-muconate. The crystal structures of the anaerobic 3,4-PCD.PCA complex, aerobic complexes with two heterocyclic PCA analogs, 2-hydroxyisonicotinic, acid N-oxide (INO) and 6-hydroxynicotinic acid N-oxide (NNO), and ternary, complexes of 3,4-PCD.INO.CN and 3,4-PCD. NNO.CN have been determined at, 2.1-2.2 A resolution and refined to R-factors between 0.165 and 0.184., PCA, INO, and NNO form very similar, asymmetrically chelated complexes, with the active site Fe3+ that result in dissociation of the endogenous, axial tyrosinate Fe3+ ligand, Tyr447 (147beta). After its release from the, ... [(full description)]
About this StructureAbout this Structure
3PCJ is a [Protein complex] structure of sequences from [Pseudomonas putida] with FE, BME and INO as [ligands]. Active as [[1]], with EC number [1.13.11.3]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding., Orville AM, Lipscomb JD, Ohlendorf DH, Biochemistry. 1997 Aug 19;36(33):10052-66. PMID:9254600
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