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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
Crystal structure of type III glutamine synthetase: Surprising reversal of the inter-ring interface
Structure, Volume 19, No. 4, Year 2011
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Description
Glutamine synthetases are ubiquitous, homo-oligomeric enzymes essential for nitrogen metabolism. Unlike types I and II, which are well described both structurally and functionally, the larger, type IIIs are poorly characterized despite their widespread occurrence. An understanding of the structural basis for this divergence and the implications for design of type-specific inhibitors has, therefore, been impossible. The first crystal structure of a GSIII enzyme, presented here, reveals a conservation of the GS catalytic fold but subtle differences in protein-ligand interactions suggest possible avenues for the design GSIII inhibitors. Despite these similarities, the divergence of the GSIII enzymes can be explained by differences in quaternary structure. Unexpectedly, the two hexameric rings of the GSIII dodecamer associate on the opposite surface relative to types I and II. The diversity of GS quaternary structures revealed here suggests a nonallosteric role for the evolution of the double-ringed architecture seen in all GS enzymes. © 2011 Elsevier Ltd. All rights reserved.
Authors & Co-Authors
van Rooyen, Jason M.
South Africa, Cape Town
University of Cape Town
Abratt, Valerie R.
South Africa, Cape Town
University of Cape Town
Belrhali, Hassan
France, Grenoble
Embl Grenoble European Molecular Biology Laboratory
Sewell, Trevor Trevor
South Africa, Cape Town
University of Cape Town
Statistics
Citations: 47
Authors: 4
Affiliations: 2
Identifiers
Doi:
10.1016/j.str.2011.02.001
ISSN:
09692126
e-ISSN:
18784186