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...

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Bibliographic Details
Published in:Nature (London) 1986-09, Vol.323 (6086), p.304-309
Main Authors: Almassy, Robert J, Janson, Cheryl A, Hamlin, R, Xuong, N-H, Eisenberg, David
Format: Article
Language:English
Subjects:
Adenine Nucleotides
Allosteric Regulation
Binding Sites
Biological and medical sciences
Catalysis
Computer Graphics
Crystalline structure
Feedback
Fundamental and applied biological sciences. Psychology
Glutamate-Ammonia Ligase - physiology
Humanities and Social Sciences
Macromolecular Substances
Models, Molecular
Molecular biophysics
multidisciplinary
Protein Conformation
Salmonella typhimurium
Science
Science (multidisciplinary)
Structure in molecular biology
X-Ray Diffraction
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/323304a0