2j9e

Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake

spinqualitylabelsall models 2j9e, resolution 1.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2j9e is a 3 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.62Å Ligands: ACT, AKG, ATP, CL, MG, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLNK1_METJA Involved in the regulation of nitrogen metabolism (PubMed:17203075). Regulates the activity of its targets by protein-protein interaction in response to the nitrogen status of the cell (PubMed:17203075). Regulates the activity of the ammonia channel Amt1 via direct interaction (PubMed:17203075). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A binary complex of the ammonia channel Amt1 from Methanococcus jannaschii and its cognate P(II) signalling protein GlnK1 has been produced and characterized. Complex formation is prevented specifically by the effector molecules Mg-ATP and 2-ketoglutarate. Single-particle electron microscopy of the complex shows that GlnK1 binds on the cytoplasmic side of Amt1. Three high-resolution X-ray structures of GlnK1 indicate that the functionally important T-loop has an extended, flexible conformation in the absence of Mg-ATP, but assumes a compact, tightly folded conformation upon Mg-ATP binding, which in turn creates a 2-ketoglutarate-binding site. We propose a regulatory mechanism by which nitrogen uptake is controlled by the binding of both effector molecules to GlnK1. At normal effector levels, a 2-ketoglutarate molecule binding at the apex of the compact T-loop would prevent complex formation, ensuring uninhibited ammonia uptake. At low levels of Mg-ATP, the extended loops would seal the ammonia channels in the complex. Binding of both effector molecules to P(II) signalling proteins may thus represent an effective feedback mechanism for regulating ammonium uptake through the membrane. Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake.,Yildiz O, Kalthoff C, Raunser S, Kuhlbrandt W EMBO J. 2007 Jan 24;26(2):589-99. Epub 2007 Jan 4. PMID:17203075 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA