5ZLI

Crystal structure of glutamine synthetase from helicobacter pylori

5ZLI の概要

• エントリーDOI: 10.2210/pdb5zli/pdb
• 分子名称: Glutamine synthetase (1 entity in total)
• 機能のキーワード: glutamine synthetase, enzyme, gs, helicobacter pylori, structural protein, ligase
• 由来する生物種: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 327477.26

構造登録者

Joo, H.K.,Lee, J.Y. (登録日: 2018-03-28, 公開日: 2018-08-29, 最終更新日: 2024-03-27)

主引用文献

Joo, H.K.,Park, Y.W.,Jang, Y.Y.,Lee, J.Y.
Structural Analysis of Glutamine Synthetase from Helicobacter pylori.
Sci Rep, 8:11657-11657, 2018

PubMed Abstract: Glutamine synthetase (GS) is an enzyme that regulates nitrogen metabolism and synthesizes glutamine via glutamate, ATP, and ammonia. GS is a homo-oligomeric protein of eight, ten, or twelve subunits, and each subunit-subunit interface has its own active site. GS can be divided into GS I, GS II, and GS III. GS I and GS III form dodecamer in bacteria and archaea, whereas GS II form decamer in eukaryotes. GS I can be further subdivided into GS I-α and GS I-β according to its sequence and regulatory mechanism. GS is an essential protein for the survival of Helicobacter pylori which its infection could promote gastroduodenal diseases. Here, we determined the crystal structures of the GS from H. pylori (Hpy GS) in its apo- and substrate-bound forms at 2.8 Å and 2.9 Å resolution, respectively. Hpy GS formed a dodecamer composed of two hexameric rings stacked face-to-face. Hpy GS, which belongs to GS I, cannot be clearly classified as either GS I-α or GS I-β based on its sequence and regulatory mechanism. In this study, we propose that Hpy GS could be classified as a new GS-I subfamily and provide structural information on the apo- and substrate-bound forms of the protein.

PubMed: 30076387
DOI: 10.1038/s41598-018-30191-5

実験手法

X-RAY DIFFRACTION (2.8 Å)