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Allosteric control of quaternary states in escherichia-coli aspartate-transcarbamylase

Academic Article
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Overview

authors

  • Stevens, Raymond
  • Lipscomb, W. N.

publication date

  • September 1990

journal

  • Biochemical and Biophysical Research Communications  Journal

abstract

  • Changes in the molecular dimensions of ATCase in the unligated T-state are an increase of 0.4 A in the separation of catalytic trimers when ATP binds. When the R-state is produced by binding of phosphonoacetamide and malonate, addition of CTP or CTP + UTP decreases the separation of catalytic trimers by 0.5 A. In the unliganded Glu239----Gln mutant, in which the T-state is destabilized so that the enzyme exists in an intermediate quaternary state, ligation of ATP transforms the mutant enzyme to the R-state, whereas CTP converts this enzyme to the T-state. Thus, this mutant is much more sensitive to heterotropic allosteric control than is the native enzyme. In this communication we propose a preliminary model based on new crystallographic results that heterotropic regulation occurs partly through control of the quaternary structure by these effectors, thus regulating catalysis.

subject areas

  • Allosteric Regulation
  • Aspartate Carbamoyltransferase
  • Escherichia coli
  • Macromolecular Substances
  • Protein Binding
  • Protein Conformation
  • X-Ray Diffraction
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Identity

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1016/0006-291x(90)90829-c

PubMed ID

  • 2222446
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Additional Document Info

start page

  • 1312

end page

  • 1318

volume

  • 171

issue

  • 3

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