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TitleThe structures of cytosolic and plastid-located glutamine synthetases from Medicago truncatula reveal a common and dynamic architecture.
Journal, issue, pagesActa Crystallogr D Biol Crystallogr, Vol. 70, Issue Pt 4, Page 981-993, Year 2014
Publish dateMar 19, 2014
AuthorsEva Torreira / Ana Rita Seabra / Hazel Marriott / Min Zhou / Óscar Llorca / Carol V Robinson / Helena G Carvalho / Carlos Fernández-Tornero / Pedro José Barbosa Pereira /
PubMed AbstractThe 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 ...The 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.
External linksActa Crystallogr D Biol Crystallogr / PubMed:24699643 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.35 - 20.0 Å
Structure data

EMDB-2581:
The structures of cytosolic and plastid-located glutamine synthetases from Medicago truncatula reveal a common and dynamic architecture
Method: EM (single particle) / Resolution: 20.0 Å

PDB-4is4:
The glutamine synthetase from the dicotyledonous plant M. truncatula is a decamer
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • medicago truncatula (barrel medic)
KeywordsLIGASE / decamer dicotyledonous

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