4BJH

Crystal Structure of the Aquifex Reactor Complex Formed by Dihydroorotase (H180A, H232A) with Dihydroorotate and Aspartate Transcarbamoylase with N-(phosphonacetyl)-L-aspartate (PALA)

Summary for 4BJH

• Entry DOI: 10.2210/pdb4bjh/pdb
• Descriptor: DIHYDROOROTASE, ASPARTATE CARBAMOYLTRANSFERASE, ZINC ION, ... (9 entities in total)
• Functional Keywords: hydrolase-transferase complex, pyrimidine biosynthesis, hydrolase/transferase
• Biological source: AQUIFEX AEOLICUS; More
• Total number of polymer chains: 2
• Total formula weight: 89175.70

Authors

Edwards, B.F.P.,Martin, P.D.,Grimley, E.,Vaishnav, A.,Fernando, R.,Brunzelle, J.S.,Cordes, M.,Evans, H.G.,Evans, D.R. (deposition date: 2013-04-18, release date: 2013-12-18, Last modification date: 2023-12-20)

Primary citation

Edwards, B.F.,Fernando, R.,Martin, P.D.,Grimley, E.,Cordes, M.,Vaishnav, A.,Brunzelle, J.S.,Evans, H.G.,Evans, D.R.
The Mononuclear Metal Center of Type-I Dihydroorotase from Aquifex Aeolicus.
Bmc Biochem., 14:36-, 2013

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.

PubMed: 24314009
DOI: 10.1186/1471-2091-14-36

Experimental method

X-RAY DIFFRACTION (2.2 Å)