2pia
From Proteopedia
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PHTHALATE DIOXYGENASE REDUCTASE: A MODULAR STRUCTURE FOR ELECTRON TRANSFER FROM PYRIDINE NUCLEOTIDES TO [2FE-2S]
Overview
Phthalate dioxygenase reductase (PDR) is a prototypical iron-sulfur, flavoprotein (36 kilodaltons) that utilizes flavin mononucleotide (FMN) to, mediate electron transfer from the two-electron donor, reduced, nicotinamide adenine nucleotide (NADH), to the one-electron acceptor, [2Fe-2S]. The crystal structure of oxidized PDR from Pseudomonas cepacia, has been analyzed at 2.0 angstrom resolution resolution; reduced PDR and, pyridine nucleotide complexes have been analyzed at 2.7 angstrom, resolution. NADH, FMN, and the [2Fe-2S] cluster, bound to distinct, domains, are brought together near a central cleft in the molecule, with, only 4.9 angstroms separating the flavin 8-methyl and a cysteine sulfur, ligated to iron. The domains that bind FMN and [2Fe-2S] are packed so that, the flavin ring and the plane of the [2Fe-2S] core are approximately, perpendicular. The [2Fe-2S] group is bound by four cysteines in a site, resembling that in plant ferredoxins, but its redox potential (-174, millivolts at pH 7.0) is much higher than the potentials of plant, ferredoxins. Structural and sequence similarities assign PDR to a distinct, family of flavoprotein reductases, all related to ferredoxin, NADP(+)-reductase.
About this Structure
2PIA is a Single protein structure of sequence from Burkholderia cepacia with FMN and FES as ligands. Full crystallographic information is available from OCA.
Reference
Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]., Correll CC, Batie CJ, Ballou DP, Ludwig ML, Science. 1992 Dec 4;258(5088):1604-10. PMID:1280857
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