1U8V

Crystal Structure of 4-Hydroxybutyryl-CoA Dehydratase from Clostridium aminobutyricum: Radical catalysis involving a [4Fe-4S] cluster and flavin

Summary for 1U8V

• Entry DOI: 10.2210/pdb1u8v/pdb
• Descriptor: Gamma-aminobutyrate metabolism dehydratase/isomerase, IRON/SULFUR CLUSTER, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: alfa-helixes, beta-strands, lyase, isomerase
• Biological source: Clostridium aminobutyricum
• Total number of polymer chains: 4
• Total formula weight: 222837.31

Authors

Martins, B.M.,Dobbek, H.,Cinkaya, I.,Buckel, W.,Messerschmidt, A. (deposition date: 2004-08-07, release date: 2004-12-21, Last modification date: 2024-02-14)

Primary citation

Martins, B.M.,Dobbek, H.,Cinkaya, I.,Buckel, W.,Messerschmidt, A.
Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis involving a [4Fe-4S] cluster and flavin.
Proc.Natl.Acad.Sci.USA, 101:15645-15649, 2004

PubMed Abstract: Dehydratases catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the elimination of water. The 1.6-A resolution crystal structure of 4-hydroxybutyryl-CoA dehydratase from the gamma-aminobutyrate-fermenting Clostridium aminobutyricum represents a new class of dehydratases with an unprecedented active site architecture. A [4Fe-4S](2+) cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide (FAD) moiety. The structure provides insight into the function of these ubiquitous prosthetic groups in the chemically nonfacile, radical-mediated dehydration of 4-hydroxybutyryl-CoA. The substrate can be bound between the [4Fe-4S](2+) cluster and the FAD with both cofactors contributing to its radical activation and catalytic conversion. Our results raise interesting questions regarding the mechanism of acyl-CoA dehydrogenases, which are involved in fatty acid oxidation, and address the divergent evolution of the ancestral common gene.

PubMed: 15496473
DOI: 10.1073/pnas.0403952101

Experimental method

X-RAY DIFFRACTION (1.6 Å)