4is4: Difference between revisions
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==The glutamine synthetase from the dicotyledonous plant M. truncatula is a decamer== | ==The glutamine synthetase from the dicotyledonous plant M. truncatula is a decamer== | ||
<StructureSection load='4is4' size='340' side='right' caption='[[4is4]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='4is4' size='340' side='right'caption='[[4is4]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4is4]] is a 10 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4is4]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_truncatula Medicago truncatula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IS4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4is4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4is4 OCA], [https://pdbe.org/4is4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4is4 RCSB], [https://www.ebi.ac.uk/pdbsum/4is4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4is4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/O04998_MEDTR O04998_MEDTR] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4is4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4is4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Medicago truncatula]] | ||
[[Category: Carvalho | [[Category: Carvalho H]] | ||
[[Category: Pereira | [[Category: Pereira PJB]] | ||
[[Category: Seabra | [[Category: Seabra AR]] | ||
Latest revision as of 18:29, 20 September 2023
The glutamine synthetase from the dicotyledonous plant M. truncatula is a decamerThe glutamine synthetase from the dicotyledonous plant M. truncatula is a decamer
Structural highlights
FunctionPublication Abstract from PubMedThe first step of nitrogen assimilation in higher plants, the energy-driven incorporation of ammonia into glutamate, is catalyzed by glutamine synthetase. This central process yields the readily metabolizable glutamine, which in turn is at the basis of all subsequent biosynthesis of nitrogenous compounds. The essential role performed by glutamine synthetase makes it a prime target for herbicidal compounds, but also a suitable intervention point for the improvement of crop yields. Although the majority of crop plants are dicotyledonous, little is known about the structural organization of glutamine synthetase in these organisms and about the functional differences between the different isoforms. Here, the structural characterization of two glutamine synthetase isoforms from the model legume Medicago truncatula is reported: the crystallographic structure of cytoplasmic GSII-1a and an electron cryomicroscopy reconstruction of plastid-located GSII-2a. Together, these structural models unveil a decameric organization of dicotyledonous glutamine synthetase, with two pentameric rings weakly connected by inter-ring loops. Moreover, rearrangement of these dynamic loops changes the relative orientation of the rings, suggesting a zipper-like mechanism for their assembly into a decameric enzyme. Finally, the atomic structure of M. truncatula GSII-1a provides important insights into the structural determinants of herbicide resistance in this family of enzymes, opening new avenues for the development of herbicide-resistant plants. The structures of cytosolic and plastid-located glutamine synthetases from Medicago truncatula reveal a common and dynamic architecture.,Torreira E, Seabra AR, Marriott H, Zhou M, Llorca O, Robinson CV, Carvalho HG, Fernandez-Tornero C, Pereira PJ Acta Crystallogr D Biol Crystallogr. 2014 Apr;70(Pt 4):981-93. doi:, 10.1107/S1399004713034718. Epub 2014 Mar 19. PMID:24699643[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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