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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Novel subunit-subunit interactions in the structure of glutamine synthetase.

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.[1]

References

  1. Novel subunit-subunit interactions in the structure of glutamine synthetase. Almassy, R.J., Janson, C.A., Hamlin, R., Xuong, N.H., Eisenberg, D. Nature (1986) [Pubmed]
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