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Título: | Arginine and nitrogen storage |
Autor: | Llácer, José Luis CSIC ORCID ; Fita, Ignacio CSIC ORCID ; Rubio, Vicente CSIC ORCID | Fecha de publicación: | dic-2008 | Editor: | Elsevier | Citación: | Current Opinion in Structural Biology 18(6): 673-681 (2008) | Resumen: | When nitrogen is abundant, prokaryotic and eukaryotic oxygen-producing photosynthetic organisms store nitrogen as arginine, by relieving feedback inhibition of the arginine biosynthesis controlling enzyme, N-acetylglutamate kinase (NAGK). The signalling protein PII, an ancient and widely distributed nitrogen/carbon/ADP/ATP sensor, mediates feedback inhibition relief of NAGK by binding to this enzyme. PII phosphorylation or PII binding of ADP or 2-oxoglutarate prevents PII-NAGK complex formation. Crystal structures of NAGK, cyanobacterial and plant PII and corresponding PII-NAGK complexes have been recently determined. In these complexes, two polar PII trimers sandwich one ring-like NAGK hexamer. Each PII subunit contacts one NAGK subunit, triggering a symmetry-restricted narrowing of the NAGK ring, with concomitant adoption by the arginine sites of a low-affinity conformation. © 2008 Elsevier Ltd. All rights reserved. | Versión del editor: | http://dx.doi.org/10.1016/j.sbi.2008.11.002 | URI: | http://hdl.handle.net/10261/111022 | DOI: | 10.1016/j.sbi.2008.11.002 | Identificadores: | doi: 10.1016/j.sbi.2008.11.002 issn: 0959-440X |
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2008 Curr Opin Struct Biol 18-673_vers_aut.pdf | 2,16 MB | Adobe PDF | Visualizar/Abrir |
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