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3pcc
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 4-HYDROXYBENZOATE
Overview
Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring, cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis, cis-muconate. Crystal structures of Pseudomonas putida3,4-PCD [quaternary, structure of (alphabetaFe3+)12] complexed with seven competitive, inhibitors [3-hydroxyphenylacetate (MHP), 4-hydroxyphenylacetate (PHP), 3-hydroxybenzoate (MHB), 4-hydroxybenzoate (PHB), 3-fluoro-4-hydroxybenzoate (FHB), 3-chloro-4-hydroxybenzoate (CHB), and, 3-iodo-4-hydroxybenzoate (IHB)] are reported at 2.0-2.2 A resolution with, R-factors of 0. 0.159-0.179. The inhibitors bind in a narrow active site, crevasse lined with residues that provide a microenvironment that closely, matches the chemical characteristics of the inhibitors. This results in as, little as 20% ... [(full description)]
About this Structure
3PCC is a [Protein complex] structure of sequences from [Pseudomonas putida] with FE, BME and PHB 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, VEA, VEB, VEC, VED, VEE and VEF. Full crystallographic information is available from [OCA].
Reference
Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site., Orville AM, Elango N, Lipscomb JD, Ohlendorf DH, Biochemistry. 1997 Aug 19;36(33):10039-51. PMID:9254599
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