Download MendeleyThe Mononuclear Metal Center of Type-I Dihydroorotase from Aquifex Aeolicus.
Edwards, B.F., Fernando, R., Martin, P.D., Grimley, E., Cordes, M., Vaishnav, A., Brunzelle, J.S., Evans, H.G., Evans, D.R.(2013) BMC Biochem 14: 36
- PubMed: 24314009
- DOI: https://doi.org/10.1186/1471-2091-14-36
- Primary Citation of Related Structures:
4BJH - PubMed Abstract:
Dihydroorotase (DHO) is a zinc metalloenzyme, although the number of active site zinc ions has been controversial. E. coli DHO was initially thought to have a mononuclear metal center, but the subsequent X-ray structure clearly showed two zinc ions, α and β, at the catalytic site. Aquifex aeolicus DHO, is a dodecamer comprised of six DHO and six aspartate transcarbamoylase (ATC) subunits. The isolated DHO monomer, which lacks catalytic activity, has an intact α-site and conserved β-site ligands, but the geometry of the second metal binding site is completely disrupted. However, the putative β-site is restored when the complex with ATC is formed and DHO activity is regained. Nevertheless, the X-ray structure of the complex revealed a single zinc ion at the active site. The structure of DHO from the pathogenic organism, S. aureus showed that it also has a single active site metal ion.
Organizational Affiliation:
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, 540 East Canfield Street, Detroit, MI 48201, USA. drevans@med.wayne.edu.
