3pca
From Proteopedia
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Revision as of 15:41, 30 October 2007
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STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 3,4-DIHYDROXYBENZOATE
Overview
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 Structure
3PCA is a [Protein complex] structure of sequences from [Pseudomonas putida] with FE, BME and DHB as [ligands]. Active as [Protocatechuate 3,4-dioxygenase], with EC number [1.13.11.3]. Structure known Active Sites: ACA, ACB, ACC, ACD, ACE, ACF, S2M, S2P, VEA, VEB, VEC, VED, VEE and VEF. Full crystallographic information is available from [OCA].
Reference
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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