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Structure paper

TitleMetal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate Transcarbamoylase.
Journal, issue, pagesBiochemistry, Vol. 51, Page 7128-7137, Year 2012
Publish dateJul 5, 2012 (structure data deposition date)
AuthorsCockrell, G.M. / Kantrowitz, E.R.
External linksBiochemistry / PubMed:22906065
MethodsX-ray diffraction
Resolution1.9395 - 2.1 Å
Structure data

PDB-4fyv:
Aspartate Transcarbamoylase Complexed with dCTP
Method: X-RAY DIFFRACTION / Resolution: 2.0976 Å

PDB-4fyw:
E. coli Aspartate Transcarbamoylase complexed with CTP
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4fyx:
E. coli Aspartate Transcarbamoylase complexed with dCTP, UTP, and Mg2+
Method: X-RAY DIFFRACTION / Resolution: 2.0889 Å

PDB-4fyy:
E. coli Aspartate Transcarbamoylase Complexed with CTP, UTP, and Mg2+
Method: X-RAY DIFFRACTION / Resolution: 1.9395 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-ZN:
Unknown entry

ChemComp-DCP:
2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE

ChemComp-HOH:
WATER

ChemComp-CTP:
CYTIDINE-5'-TRIPHOSPHATE

ChemComp-UTP:
URIDINE 5'-TRIPHOSPHATE / UTP*YM

ChemComp-MG:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / Allosteric Regulation / Aspartate Carbamoyltransferase / Escherichia coli / pyrimidine nucleotide biosynthesis / feedback inhibition / allostery

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