Crystal structure of Type III glutamine synthetase: surprising reversal of the inter-ring interface
| dc.contributor.author | van Rooyen, Jason M | |
| dc.contributor.author | Abratt, Valerie R | |
| dc.contributor.author | Belrhali, Hassan | |
| dc.contributor.author | Sewell, Trevor | |
| dc.date.accessioned | 2016-09-01T09:54:55Z | |
| dc.date.available | 2016-09-01T09:54:55Z | |
| dc.date.issued | 2011 | |
| dc.date.updated | 2016-09-01T09:53:48Z | |
| dc.description.abstract | 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. | en_ZA |
| dc.identifier | http://dx.doi.org/10.1016/j.str.2011.02.001 | |
| dc.identifier.apacitation | van Rooyen, J. M., Abratt, V. R., Belrhali, H., & Sewell, T. (2011). Crystal structure of Type III glutamine synthetase: surprising reversal of the inter-ring interface. <i>Structure</i>, http://hdl.handle.net/11427/21640 | en_ZA |
| dc.identifier.chicagocitation | van Rooyen, Jason M, Valerie R Abratt, Hassan Belrhali, and Trevor Sewell "Crystal structure of Type III glutamine synthetase: surprising reversal of the inter-ring interface." <i>Structure</i> (2011) http://hdl.handle.net/11427/21640 | en_ZA |
| dc.identifier.citation | van Rooyen, J. M., Abratt, V. R., Belrhali, H., & Sewell, T. (2011). Crystal structure of type III glutamine synthetase: Surprising reversal of the inter-ring interface. Structure, 19(4), 471-483. | en_ZA |
| dc.identifier.issn | 0969-2126 | en_ZA |
| dc.identifier.ris | TY - Journal Article AU - van Rooyen, Jason M AU - Abratt, Valerie R AU - Belrhali, Hassan AU - Sewell, Trevor AB - 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. DA - 2011 DB - OpenUCT DP - University of Cape Town J1 - Structure LK - https://open.uct.ac.za PB - University of Cape Town PY - 2011 SM - 0969-2126 T1 - Crystal structure of Type III glutamine synthetase: surprising reversal of the inter-ring interface TI - Crystal structure of Type III glutamine synthetase: surprising reversal of the inter-ring interface UR - http://hdl.handle.net/11427/21640 ER - | en_ZA |
| dc.identifier.uri | http://hdl.handle.net/11427/21640 | |
| dc.identifier.uri | http://www.cell.com/structure/abstract/S0969-2126(11)00069-4 | |
| dc.identifier.vancouvercitation | van Rooyen JM, Abratt VR, Belrhali H, Sewell T. Crystal structure of Type III glutamine synthetase: surprising reversal of the inter-ring interface. Structure. 2011; http://hdl.handle.net/11427/21640. | en_ZA |
| dc.language | eng | en_ZA |
| dc.publisher | Elsevier | en_ZA |
| dc.publisher.institution | University of Cape Town | |
| dc.source | Structure | en_ZA |
| dc.source.uri | http://www.cell.com/structure/home | |
| dc.subject.other | Crystal Structure | |
| dc.subject.other | Type III Glutamine Synthetase | |
| dc.subject.other | Inter-Ring Interface | |
| dc.title | Crystal structure of Type III glutamine synthetase: surprising reversal of the inter-ring interface | en_ZA |
| dc.type | Journal Article | en_ZA |
| uct.type.filetype | Text | |
| uct.type.filetype | Image | |
| uct.type.publication | Research | en_ZA |
| uct.type.resource | Article | en_ZA |