Publication Abstract from PubMed
X-ray crystallography and small-angle X-ray scattering (SAXS) in solution have been used to show that a mutant aspartate transcarbamoylase exists in an intermediate quaternary structure between the canonical T and R structures. Additionally, the SAXS data indicate a pH-dependent structural alteration consistent with either a pH-induced conformational change or a pH-induced alteration in the T to R equilibrium. These data indicate that this mutant is not a model for the R state, as has been proposed, but rather represents the enzyme trapped along the path of the allosteric transition between the T and R states.
Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase.,Guo W, West JM, Dutton AS, Tsuruta H, Kantrowitz ER Proc Natl Acad Sci U S A. 2012 Apr 30. PMID:22547808[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
