3O8W: Archaeoglobus Fulgidus Glnk1

Citation:
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2011) 67 p.178-181
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 A 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.
PDB ID: 3O8WDownload
MMDB ID: 88538
PDB Deposition Date: 2010/8/3
Updated in MMDB: 2011/05
Experimental Method:
x-ray diffraction
Resolution: 2.28  Å
Source Organism:
Similar Structures:
Biological Unit for 3O8W: trimeric; determined by author and by software (PISA)
Molecular Components in 3O8W
Label Count Molecule
Proteins (3 molecules)
3
Nitrogen Regulatory Protein P-ii (Glnb-1)
Molecule annotation
Chemicals (6 molecules)
1
6
* Click molecule labels to explore molecular sequence information.

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