Llácer José L, Fita Ignacio, Rubio Vicente
Instituto de Biomedicina de Valencia-Consejo Superior de Investigaciones Cientificas (IBV-CSIC) and Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER-ISCIII), Jaime Roig 11, Valencia 46010, Spain.
Curr Opin Struct Biol. 2008 Dec;18(6):673-81. doi: 10.1016/j.sbi.2008.11.002. Epub 2008 Nov 27.
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.
当氮充足时,原核和真核产氧光合生物通过解除对精氨酸生物合成控制酶N - 乙酰谷氨酸激酶(NAGK)的反馈抑制,将氮储存为精氨酸。信号蛋白PII是一种古老且广泛分布的氮/碳/ADP/ATP传感器,通过与该酶结合介导NAGK反馈抑制的解除。PII的磷酸化或PII与ADP或2 - 酮戊二酸的结合会阻止PII - NAGK复合物的形成。最近已经确定了NAGK、蓝细菌和植物PII以及相应的PII - NAGK复合物的晶体结构。在这些复合物中,两个极性PII三聚体夹着一个环状NAGK六聚体。每个PII亚基与一个NAGK亚基接触,引发NAGK环对称性受限的变窄,同时精氨酸位点采用低亲和力构象。