7P50

GlnK2 from Methanothermococcus thermolithotrophicus in complex with Mg-ATP and 2-oxoglutarate at a resolution of 1.16 A

これはPDB形式変換不可エントリーです。

7P50 の概要

• エントリーDOI: 10.2210/pdb7p50/pdb
• 分子名称: GlnK2 from Methanothermococcus thermolithotrophicus, 2-OXOGLUTARIC ACID, MAGNESIUM ION, ... (8 entities in total)
• 機能のキーワード: pii-family, methanococcales, methanogenic archaea, thermophile, hydrogenotrophic, protein regulation, inhibitor, conformational change, atp, 2-oxoglutarate, t-loop, signaling protein
• 由来する生物種: Methanothermococcus thermolithotrophicus DSM 2095
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 46542.58

構造登録者

Mueller, M.-C.,Wagner, T. (登録日: 2021-07-13, 公開日: 2021-10-06, 最終更新日: 2024-01-31)

主引用文献

Muller, M.C.,Wagner, T.
The Oxoglutarate Binding Site and Regulatory Mechanism Are Conserved in Ammonium Transporter Inhibitors GlnKs from Methanococcales .
Int J Mol Sci, 22:-, 2021

PubMed Abstract: Protein inhibition is a natural regulatory process to control cellular metabolic fluxes. P-family signal-transducing effectors are in this matter key regulators of the nitrogen metabolism. Their interaction with their various targets is governed by the cellular nitrogen level and the energy charge. Structural studies on GlnK, a P-family inhibitor of the ammonium transporters (Amt), showed that the T-loops responsible for channel obstruction are displaced upon the binding of 2-oxoglutarate, magnesium and ATP in a conserved cleft. However, GlnK from was shown to bind 2-oxoglutarate on the tip of its T-loop, causing a moderate disruption to GlnK-Amt interaction, raising the question if methanogenic archaea use a singular adaptive strategy. Here we show that membrane fractions of released GlnKs only in the presence of Mg-ATP and 2-oxoglutarate. This observation led us to structurally characterize the two GlnK isoforms apo or in complex with ligands. Together, our results show that the 2-oxoglutarate binding interface is conserved in GlnKs from , including , emphasizing the importance of a free carboxy-terminal group to facilitate ligand binding and to provoke the shift of the T-loop positions.

PubMed: 34445335
DOI: 10.3390/ijms22168631

実験手法

X-RAY DIFFRACTION (1.16 Å)