8JZH

C. glutamicum S-adenosylmethionine synthase

8JZH の概要

• エントリーDOI: 10.2210/pdb8jzh/pdb
• 分子名称: S-adenosylmethionine synthase, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• 機能のキーワード: s-adenosylmethionine synthase, complex, sam, transferase
• 由来する生物種: Corynebacterium glutamicum ATCC 13032
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 136034.86

構造登録者

Lee, S.,Kim, K.J. (登録日: 2023-07-05, 公開日: 2023-10-25, 最終更新日: 2023-11-08)

主引用文献

Lee, S.,Kim, S.,Kim, I.K.,Kim, K.J.
Structural and Biochemical Studies on Product Inhibition of S-Adenosylmethionine Synthetase from Corynebacterium glutamicum .
J.Agric.Food Chem., 71:15692-15700, 2023

PubMed Abstract: S-Adenosylmethionine (SAM) acts as a methyl donor in living organisms, and S-adenosylmethionine synthetase (MetK) is an essential enzyme for cells, as it synthesizes SAM from methionine and adenosine triphosphate (ATP). This study determined the crystal structures of the apo form and adenosine/triphosphate complex form of MetK from (MetK). Results showed that MetK has an allosteric inhibitor binding site for the SAM product in the vicinity of the active site and is inhibited by SAM both competitively and noncompetitively. Through structure-guided protein engineering, the MetK variant was developed that exhibited an almost complete release of inhibition by SAM with rather enhanced enzyme activity. The crystal structure of the MetK variant revealed that the formation of a new hydrogen bond between Tyr66 and Glu102 by the E68A mutation disrupted the allosteric SAM binding site and also improved the protein thermal stability by strengthening the tetramerization of the enzyme.

PubMed: 37846083
DOI: 10.1021/acs.jafc.3c05180

実験手法

X-RAY DIFFRACTION (2.2 Å)