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TitleA Single Amino Acid Substitution in the Active Site of Escherichia coli Aspartate Transcarbamoylase Prevents the Allosteric Transition.
Journal, issue, pagesJ. Mol. Biol., Vol. 349, Page 413-423, Year 2005
Publish dateSep 25, 2004 (structure data deposition date)
AuthorsStieglitz, K.A. / Pastra-Landis, S.C. / Xia, J. / Tsuruta, H. / Kantrowitz, E.R.
External linksJ. Mol. Biol. / PubMed:15890205
MethodsX-ray diffraction
Resolution2.71 Å
Structure data

PDB-1xjw:
The Structure of E. coli Aspartate Transcarbamoylase Q137A Mutant in The R-State
Method: X-RAY DIFFRACTION / Resolution: 2.71 Å

Chemicals

ChemComp-PAL:
N-(PHOSPHONACETYL)-L-ASPARTIC ACID

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE/TRANSFERASE REGULATOR / Allosteric enzyme / polar contacts / electrostatics / small angle x-ray scattering / domain closure / intersubunit interactions / TRANSFERASE-TRANSFERASE REGULATOR COMPLEX

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