8UFJ

Structure of M. mazei GS(R167L-A168G) apo form

これはPDB形式変換不可エントリーです。

8UFJ の概要

• エントリーDOI: 10.2210/pdb8ufj/pdb
• 分子名称: Glutamine synthetase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: glutamine synthetase, methanosarcina mazei, gs, glnk, dodecamer, ligase
• 由来する生物種: Methanosarcina mazei Go1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 158455.42

構造登録者

Schumacher, M.A. (登録日: 2023-10-04, 公開日: 2023-11-15, 最終更新日: 2023-11-29)

主引用文献

Schumacher, M.A.,Salinas, R.,Travis, B.A.,Singh, R.R.,Lent, N.
M. mazei glutamine synthetase and glutamine synthetase-GlnK1 structures reveal enzyme regulation by oligomer modulation.
Nat Commun, 14:7375-7375, 2023

PubMed Abstract: Glutamine synthetases (GS) play central roles in cellular nitrogen assimilation. Although GS active-site formation requires the oligomerization of just two GS subunits, all GS form large, multi-oligomeric machines. Here we describe a structural dissection of the archaeal Methanosarcina mazei (Mm) GS and its regulation. We show that Mm GS forms unstable dodecamers. Strikingly, we show this Mm GS oligomerization property is leveraged for a unique mode of regulation whereby labile Mm GS hexamers are stabilized by binding the nitrogen regulatory protein, GlnK1. Our GS-GlnK1 structure shows that GlnK1 functions as molecular glue to affix GS hexamers together, stabilizing formation of GS active-sites. These data, therefore, reveal the structural basis for a unique form of enzyme regulation by oligomer modulation.

PubMed: 37968329
DOI: 10.1038/s41467-023-43243-w

実験手法

X-RAY DIFFRACTION (2.45 Å)