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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Almassy, R., Janson, C., Hamlin, R. et al. Novel subunit—subunit interactions in the structure of glutamine synthetase. Nature 323, 304–309 (1986). https://doi.org/10.1038/323304a0
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DOI: https://doi.org/10.1038/323304a0
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