PMID:2876389

Citation	Almassy, RJ, Janson, CA, Hamlin, R, Xuong, NH and Eisenberg, D Novel subunit-subunit interactions in the structure of glutamine synthetase. Nature 323:304-9
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.
Links	PubMed Online version:10.1038/323304a0
Keywords	Adenine Nucleotides; Allosteric Regulation; Binding Sites; Catalysis; Computer Graphics; Feedback; Glutamate-Ammonia Ligase/physiology; Macromolecular Substances; Models, Molecular; Protein Conformation; Salmonella typhimurium; X-Ray Diffraction
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