Novel subunit—subunit interactions in the structure of glutamine synthetase

Authors:
  • RARobert J. Almassy
    Robert J. Almassy
  • CJCheryl A. Janson
    Cheryl A. Janson
  • RHR. Hamlin
    R. Hamlin
  • NXN-H. Xuong
    N-H. Xuong
  • DEDavid Eisenberg
    David Eisenberg

Abstract
We present an atomic model for glutamine synthetase, an enzyme of central importance in bacterial nitrogen metabolism, from X-ray crystallography. The 12 identical subunits are arranged as the carbon atoms in two face-to-face benzene rings, with unusual subunit contacts. Our model, which places the active sites at the subunit interfaces, suggests a mechanism for the main functional role of glutamine synthetase: how the enzyme regulates the rate of synthesis of glutamine in response to covalent modification and feedback inhibition.

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