2PIA

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

2PIA の概要

• エントリーDOI: 10.2210/pdb2pia/pdb
• 分子名称: PHTHALATE DIOXYGENASE REDUCTASE, FLAVIN MONONUCLEOTIDE, FE2/S2 (INORGANIC) CLUSTER, ... (4 entities in total)
• 機能のキーワード: reductase
• 由来する生物種: Burkholderia cepacia
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36212.01

構造登録者

Correll, C.C.,Batie, C.J.,Ballou, D.P.,Ludwig, M.L. (登録日: 1993-02-15, 公開日: 1993-04-15, 最終更新日: 2024-02-21)

主引用文献

Correll, C.C.,Batie, C.J.,Ballou, D.P.,Ludwig, M.L.
Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S].
Science, 258:1604-1610, 1992

PubMed Abstract: 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.

PubMed: 1280857

実験手法

X-RAY DIFFRACTION (2 Å)