1SB3

Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica

Summary for 1SB3

• Entry DOI: 10.2210/pdb1sb3/pdb
• Related: 1RM6
• Descriptor: 4-hydroxybenzoyl-CoA reductase alpha subunit, 4-hydroxybenzoyl-CoA reductase beta subunit, 4-hydroxybenzoyl-CoA reductase gamma subunit, ... (10 entities in total)
• Functional Keywords: xanthine oxidase family, dimer of heterotrimers, (a, b, c)2, oxidoreductase
• Biological source: Thauera aromatica; More
• Total number of polymer chains: 6
• Total formula weight: 273096.46

Authors

Unciuleac, M.,Warkentin, E.,Page, C.C.,Boll, M.,Ermler, U. (deposition date: 2004-02-10, release date: 2004-12-21, Last modification date: 2023-08-23)

Primary citation

Unciuleac, M.,Warkentin, E.,Page, C.C.,Boll, M.,Ermler, U.
Structure of a Xanthine Oxidase-Related 4-Hydroxybenzoyl-CoA Reductase with an Additional [4Fe-4S] Cluster and an Inverted Electron Flow.
Structure, 12:2249-2256, 2004

PubMed Abstract: The Mo-flavo-Fe/S-dependent heterohexameric protein complex 4-hydroxybenzoyl-CoA reductase (4-HBCR, dehydroxylating) is a central enzyme of the anaerobic degradation of phenolic compounds and belongs to the xanthine oxidase (XO) family of molybdenum enzymes. Its X-ray structure was established at 1.6 A resolution. The most pronounced difference between 4-HBCR and other structurally characterized members of the XO family is the insertion of 40 amino acids within the beta subunit, which carries an additional [4Fe-4S] cluster at a distance of 16.5 A to the isoalloxazine ring of FAD. The architecture of 4-HBCR and concomitantly performed electron transfer rate calculations suggest an inverted electron transfer chain from the donor ferredoxin via the [4Fe-4S] cluster to the Mo over a distance of 55 A. The binding site of 4-hydroxybenzoyl-CoA is located in an 18 A long channel lined up by several aromatic side chains around the aromatic moiety, which are proposed to shield and stabilize the postulated radical intermediates during catalysis.

PubMed: 15576037
DOI: 10.1016/j.str.2004.10.008

Experimental method

X-RAY DIFFRACTION (2.2 Å)