1RGV

Crystal Structure of the Ferredoxin from Thauera aromatica

1RGV の概要

• エントリーDOI: 10.2210/pdb1rgv/pdb
• 分子名称: ferredoxin, IRON/SULFUR CLUSTER (2 entities in total)
• 機能のキーワード: electron transport
• 由来する生物種: Thauera aromatica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9667.18

構造登録者

Unciuleac, M.,Boll, M.,Warkentin, E.,Ermler, U. (登録日: 2003-11-13, 公開日: 2004-02-10, 最終更新日: 2023-08-23)

主引用文献

Unciuleac, M.,Boll, M.,Warkentin, E.,Ermler, U.
Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin.
Acta Crystallogr.,Sect.D, 60:388-391, 2004

PubMed Abstract: 4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a central enzyme in the metabolism of phenolic compounds in anaerobic bacteria. The enzyme catalyzes the reductive removal of the phenolic hydroxyl group from 4-hydroxybenzoyl-CoA, yielding benzoyl-CoA and water. 4-HBCR belongs to the xanthine oxidase (XO) family of molybdenum enzymes which occur as heterodimers, (alphabetagamma)(2). 4-HBCR contains two molybdopterins, four [2Fe-2S] and two [4Fe-4S] clusters and two FADs. A low-potential Allochromatium vinosum-type ferredoxin containing two [4Fe-4S] clusters serves as an in vivo electron donor for 4-HBCR. In this work, the oxygen-sensitive proteins 4-HBCR and the ferredoxin (TaFd) from Thauera aromatica were crystallized under anaerobic conditions. 4-HBCR crystallized with PEG 4000 and MPD as precipitant diffracted to about 1.6 A resolution and the crystals were highly suitable for X-ray structure analysis. Crystals of TaFd were obtained with (NH(4))(3)PO(4) as precipitant and revealed a solvent content of 77%, which is remarkably high for a small soluble protein. The structure of TaFd was solved at 2.9 A resolution by the molecular-replacement method using the highly related structure of the ferredoxin (CvFd) from A. vinosum as a model. Structural changes between the two ferredoxins around the [4Fe-4S] cluster can be correlated with their different redox potentials.

PubMed: 14747735
DOI: 10.1107/S0907444903028506

実験手法

X-RAY DIFFRACTION (2.9 Å)