1R74

Crystal Structure of Human Glycine N-Methyltransferase

1R74 の概要

• エントリーDOI: 10.2210/pdb1r74/pdb
• 分子名称: Glycine N-methyltransferase, BETA-MERCAPTOETHANOL, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: glycine n-methyltransferase, human, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q14749
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66002.90

構造登録者

Pakhomova, S.,Luka, Z.,Wagner, C.,Newcomer, M.E. (登録日: 2003-10-17, 公開日: 2004-09-21, 最終更新日: 2023-08-23)

主引用文献

Pakhomova, S.,Luka, Z.,Grohmann, S.,Wagner, C.,Newcomer, M.E.
Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes.
Proteins, 57:331-337, 2004

PubMed Abstract: Glycine N-methyltransferases (GNMTs) from three mammalian sources were compared with respect to their crystal structures and kinetic parameters. The crystal structure for the rat enzyme was published previously. Human and mouse GNMT were expressed in Escherichia coli in order to determine their crystal structures. Mouse GNMT was crystallized in two crystal forms, a monoclinic form and a tetragonal form. Comparison of the three structures reveals subtle differences, which may relate to the different kinetic properties of the enzymes. The flexible character of several loops surrounding the active site, along with an analysis of the active site boundaries, indicates that the observed conformations of human and mouse GNMTs are more open than that of the rat enzyme. There is an increase in kcat when going from rat to mouse to human, suggesting a correlation with the increased flexibility of some structural elements of the respective enzymes.

PubMed: 15340920
DOI: 10.1002/prot.20209

実験手法

X-RAY DIFFRACTION (2.55 Å)