Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study.

Lignende værker

• Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate.
  af: Krause, K L, et al.
  Udgivet: (1985)
• Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution.
  af: Ke, H M, et al.
  Udgivet: (1984)
• Interactions of metal-nucleotide complexes with aspartate carbamoyltransferase in the crystalline state.
  af: Honzatko, R B, et al.
  Udgivet: (1982)
• A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.
  af: Honzatko, R B, et al.
  Udgivet: (1979)
• Crystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure.
  af: Gouaux, J E, et al.
  Udgivet: (1989)