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Title

Arginine and nitrogen storage

AuthorsLlácer, José Luis ; Fita, Ignacio ; Rubio, Vicente
Issue DateDec-2008
PublisherElsevier
CitationCurrent Opinion in Structural Biology 18(6): 673-681 (2008)
AbstractWhen 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.
Publisher version (URL)http://dx.doi.org/10.1016/j.sbi.2008.11.002
URIhttp://hdl.handle.net/10261/111022
DOI10.1016/j.sbi.2008.11.002
Identifiersdoi: 10.1016/j.sbi.2008.11.002
issn: 0959-440X
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