Title |
The mononuclear metal center of type-I dihydroorotase from aquifex aeolicus
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Published in |
BMC Molecular and Cell Biology, December 2013
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DOI | 10.1186/1471-2091-14-36 |
Pubmed ID | |
Authors |
Brian FP Edwards, Roshini Fernando, Philip D Martin, Edward Grimley, Melissa Cordes, Asmita Vaishnav, Joseph S Brunzelle, Hedeel Guy Evans, David R Evans |
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. |
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United States | 1 | 100% |
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Members of the public | 1 | 100% |
Mendeley readers
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Professor | 2 | 20% |
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