Novel subunit—subunit interactions in the structure of glutamine synthetase
- 1 September 1986
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 323 (6086) , 304-309
- https://doi.org/10.1038/323304a0
Abstract
We present an atomic model for glutamine synthetase, an enzyme of central importance in bacterial [Salmonella typhimurium] 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.This publication has 46 references indexed in Scilit:
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