3pcn

From Proteopedia

Revision as of 06:22, 30 October 2007

STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETATE

Overview

The crystal structure of the anaerobic complex of Pseudomonas putida, protocatechuate 3,4-dioxygenase (3,4-PCD) bound with the alternative, substrate, 3,4-dihydroxyphenylacetate (HPCA), is reported at 2.4 A, resolution and refined to an R factor of 0.17. Formation of the active, site Fe(III).HPCA chelated complex causes the endogenous axial tyrosinate, Tyr447 (147beta), to dissociate from the iron and rotate into an, alternative orientation analogous to that previously observed in the, anaerobic 3,4-PCD.3,4-dihydroxybenzoate complex (3, 4-PCD.PCA) [Orville, A. M., Lipscomb, J. D., & Ohlendorf, D. H. (1997) Biochemistry 36, 10052-10066]. Two orientations of the aromatic ring of HPCA related by an, approximate 180 degrees rotation within the active site are consistent, with the electron ... [(full description)]

About this Structure

3PCN is a [Protein complex] structure of sequences from [Pseudomonas putida] with FE, BME and DHY as [ligands]. Active as [Oxidoreductase], 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

Crystal structure and resonance Raman studies of protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate., Elgren TE, Orville AM, Kelly KA, Lipscomb JD, Ohlendorf DH, Que L Jr, Biochemistry. 1997 Sep 23;36(38):11504-13. PMID:9298971

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