2GLT

STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0.

「1GLT」から置き換えられました

2GLT の概要

• エントリーDOI: 10.2210/pdb2glt/pdb
• 分子名称: GLUTATHIONE BIOSYNTHETIC LIGASE (2 entities in total)
• 機能のキーワード: glutathione biosynthesis ligase, biosynthesis, ligase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35601.82

構造登録者

Matsuda, K.,Yamaguchi, H.,Kato, H.,Nishioka, T.,Katsube, Y.,Oda, J. (登録日: 1995-05-16, 公開日: 1995-07-31, 最終更新日: 2024-05-29)

主引用文献

Matsuda, K.,Mizuguchi, K.,Nishioka, T.,Kato, H.,Go, N.,Oda, J.
Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins.
Protein Eng., 9:1083-1092, 1996

PubMed Abstract: The crystal structure of Escherichia coli B glutathione synthetase (GSHase) has been determined at the optimal catalytic condition pH 7.5. The most significant structural difference from the structure at pH 6.0 is the movement of the central domain towards the N-terminal domain almost as a rigid body. As a result of this movement, new interdomain and intersubunit polar interactions are formed which stabilize the dimeric structure further. The structure of GSHase at optimal pH was compared with 294 other known protein structures in terms of the spatial arrangements of secondary structural elements. Three enzymes (D-alanine: D-alanine ligase, succinyl-CoA synthetase and the biotin carboxylase subunit of acetyl-CoA carboxylase) were found to have structures similar to the ATP-binding site of GSHase, which extends across two domains. The ATP-binding sites in these four enzymes are composed of two antiparallel beta-sheets and are different from the classic mononucleotide-binding fold. Except for these proteins, no significant structural similarity was detected between GSHase and the other ATP-binding proteins. A structural motif in the N-terminal domain of GSHase has been found to be similar to the NAD-binding fold. This structural motif is shared by a number of other proteins that bind various negatively charged molecules.

PubMed: 9010922
DOI: 10.1093/protein/9.12.1083

実験手法

X-RAY DIFFRACTION (2.2 Å)