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TitleDihydroorotase from the hyperthermophile Aquifiex aeolicus is activated by stoichiometric association with aspartate transcarbamoylase and forms a one-pot reactor for pyrimidine biosynthesis.
Journal, issue, pagesBiochemistry, Vol. 48, Page 766-778, Year 2009
Publish dateMay 20, 2008 (structure data deposition date)
AuthorsZhang, P. / Martin, P.D. / Purcarea, C. / Vaishnav, A. / Brunzelle, J.S. / Fernando, R. / Guy-Evans, H.I. / Evans, D.R. / Edwards, B.F.
External linksBiochemistry / PubMed:19128030
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-3d6n:
Crystal Structure of Aquifex Dihydroorotase Activated by Aspartate Transcarbamoylase
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-FLC:
CITRATE ANION

ChemComp-HOH:
WATER

Source
  • aquifex aeolicus (bacteria)
KeywordsHYDROLASE/TRANSFERASE / REACTOR / CHAMBER / PORES / INTERNAL CAVITY / Hydrolase / Metal-binding / Pyrimidine biosynthesis / Transferase / HYDROLASE-TRANSFERASE COMPLEX

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