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

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.

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 Creators:
Unciuleac, Mihaela1, Author
Boll, Matthias1, Author
Warkentin, Eberhard2, Author           
Ermler, Ulrich2, Author           
Affiliations:
1Institut für Biologie II, Mikrobiologie, 79104 Freiburg, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: 4-hydroxybenzoyl-CoA reductase; ferrodoxin
 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.

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Language(s): eng - English
 Dates: 2004-01-232004-02
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S0907444903028506
PMID: 14747735
 Degree: -

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Title: Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
  Other : Acta Crystallogr D
Source Genre: Journal
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Publ. Info: [Copenhagen, Denmark : Published for the International Union of Crystallography by Munksgaard]
Pages: - Volume / Issue: 60 Sequence Number: - Start / End Page: 388 - 391 Identifier: ISSN: 0907-4449
CoNE: https://pure.mpg.de/cone/journals/resource/954925562619