2J9C
Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake
2J9C の概要
エントリーDOI | 10.2210/pdb2j9c/pdb |
関連するPDBエントリー | 2J9D 2J9E |
分子名称 | HYPOTHETICAL NITROGEN REGULATORY PII-LIKE PROTEIN MJ0059, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (7 entities in total) |
機能のキーワード | em single particle, nitrogen metabolism, signalling, transcription, membrane transport, hypothetical protein, transcription regulation |
由来する生物種 | METHANOCOCCUS JANNASCHII |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 42096.08 |
構造登録者 | Yildiz, O.,Kalthoff, C.,Raunser, S.,Kuehlbrandt, W. (登録日: 2006-11-07, 公開日: 2007-01-16, 最終更新日: 2023-12-13) |
主引用文献 | Yildiz, O.,Kalthoff, C.,Raunser, S.,Kuhlbrandt, W. Structure of Glnk1 with Bound Effectors Indicates Regulatory Mechanism for Ammonia Uptake. Embo J., 26:589-, 2007 Cited by PubMed Abstract: 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. PubMed: 17203075DOI: 10.1038/SJ.EMBOJ.7601492 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.3 Å) |
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