2pia

PHTHALATE DIOXYGENASE REDUCTASE: A MODULAR STRUCTURE FOR ELECTRON TRANSFER FROM PYRIDINE NUCLEOTIDES TO [2FE-2S]

spinqualitylabelsall models 2pia, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pia is a 1 chain structure with sequence from Burkholderia cepacia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: FES, FMN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PDR_BURCE Component of the electron transfer chain involved in pyridine nucleotide-dependent dihydroxylation of phthalate. Utilizes FMN to mediate electron transfer from the two-electron donor, NADH, to the one-electron acceptor, (2Fe-2S). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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