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TitleUse of L-asparagine and N-phosphonacetyl-L-asparagine to investigate the linkage of catalysis and homotropic cooperativity in E. coli aspartate transcarbomoylase.
Journal, issue, pagesProteins, Vol. 71, Page 1088-1096, Year 2008
Publish dateOct 12, 2006 (structure data deposition date)
AuthorsCardia, J.P. / Eldo, J. / Xia, J. / O'Day, E.M. / Tsuruta, H. / Gryncel, K.R. / Kantrowitz, E.R.
External linksProteins / PubMed:18004787
MethodsX-ray diffraction
Resolution2.6 Å
Structure data

PDB-2ipo:
E. coli Aspartate Transcarbamoylase complexed with N-phosphonacetyl-L-asparagine
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-1IP:
N~2~-(PHOSPHONOACETYL)-L-ASPARAGINE

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-ZN:
Unknown entry

ChemComp-MAE:
MALEIC ACID

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / Aspartate transcarbamoylase / allosteric / inhibitor design / domain closure

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