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1rgv
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(New page: 200px<br /><applet load="1rgv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rgv, resolution 2.90Å" /> '''Crystal Structure of...)
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Revision as of 20:32, 24 November 2007
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Crystal Structure of the Ferredoxin from Thauera aromatica
Overview
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.
About this Structure
1RGV is a Single protein structure of sequence from Thauera aromatica with SF4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin., Unciuleac M, Boll M, Warkentin E, Ermler U, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):388-91. Epub 2004, Jan 23. PMID:14747735
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