3O8W

Archaeoglobus fulgidus GlnK1

Summary for 3O8W

• Entry DOI: 10.2210/pdb3o8w/pdb
• Descriptor: Nitrogen regulatory protein P-II (GlnB-1), ACETATE ION (3 entities in total)
• Functional Keywords: signaling protein
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 1
• Total formula weight: 13296.35

Authors

Litz, C.,Helfmann, S.,Gerhardt, S.,Andrade, S.L.A. (deposition date: 2010-08-03, release date: 2011-02-09, Last modification date: 2023-09-06)

Primary citation

Litz, C.,Helfmann, S.,Gerhardt, S.,Andrade, S.L.
Structure of GlnK1, a signalling protein from Archaeoglobus fulgidus.
Acta Crystallogr.,Sect.F, 67:178-181, 2011

PubMed Abstract: GlnB and GlnK are ancient signalling proteins that play a crucial role in the regulation of nitrogen assimilation. Both protein types can be present in the same genome as either single or multiple copies. However, the gene product of glnK is always found in an operon together with an amt gene encoding an ammonium-transport (Amt) protein. Complex formation between GlnK and Amt blocks ammonium uptake and depends on the nitrogen level in the cell, which is regulated through the binding of specific effector molecules to GlnK. In particular, an ammonium shock to a cell culture previously starved in this nitrogen source or the binding of ATP to purified GlnK can stimulate effective complex formation. While the binding of ATP/ADP and 2-oxoglutarate (as a signal for low intracellular nitrogen) to GlnK have been reported and several GlnB/K protein structures are available, essential functional questions remain unanswered. Here, the crystal structure of A. fulgidus GlnK1 at 2.28 Å resolution and a comparison with the crystal structures of other GlnK proteins, in particular with that of its paralogue GlnK2 from the same organism, is reported.

PubMed: 21301082
DOI: 10.1107/S1744309110047482

Experimental method

X-RAY DIFFRACTION (2.28 Å)