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Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin

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Warkentin,  Eberhard
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Unciuleac, M., Boll, M., Warkentin, E., & Ermler, U. (2004). Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), 60, 388-391. doi:10.1107/S0907444903028506.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DAD8-7
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, ([alpha][beta][gamma])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 Å resolution and the crystals were highly suitable for X-ray structure analysis. Crystals of TaFd were obtained with (NH4)3PO4 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 Å 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.