2LGS

FEEDBACK INHIBITION OF FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM BY GLYCINE, ALANINE, AND SERINE

2LGS の概要

• エントリーDOI: 10.2210/pdb2lgs/pdb
• 分子名称: GLUTAMINE SYNTHETASE, MANGANESE (II) ION, GLUTAMIC ACID (3 entities in total)
• 機能のキーワード: ligase(amide synthetase)
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Cytoplasm: P06201
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 624017.08

構造登録者

Liaw, S.-H.,Eisenberg, D. (登録日: 1994-08-05, 公開日: 1994-11-30, 最終更新日: 2024-02-21)

主引用文献

Liaw, S.H.,Pan, C.,Eisenberg, D.
Feedback inhibition of fully unadenylylated glutamine synthetase from Salmonella typhimurium by glycine, alanine, and serine.
Proc.Natl.Acad.Sci.USA, 90:4996-5000, 1993

PubMed Abstract: Bacterial glutamine synthetase (GS; EC 6.3.1.2) was previously shown to be inhibited by nine end products of glutamine metabolism. Here we present four crystal structures of GS, complexed with the substrate Glu and with each of three feedback inhibitors. The GS of the present study is from Salmonella typhimurium, with Mn2+ ions bound, and is fully unadenylylated. From Fourier difference maps, we find that L-serine, L-alanine, and glycine bind at the site of the substrate L-glutamate. In our model, these four amino acids bind with the atoms they share in common (the "main chain" +NH3-CH-COO-) in the same positions. Thus on the basis of our x-ray work, glycine, alanine, and serine appear to inhibit GS-Mn by competing with the substrate glutamate for the active site.

PubMed: 8099447
DOI: 10.1073/pnas.90.11.4996

実験手法

X-RAY DIFFRACTION (2.8 Å)