3RY7

Crystal Structure of Sa239

3RY7 の概要

• エントリーDOI: 10.2210/pdb3ry7/pdb
• 分子名称: Ribokinase, GLYCEROL (3 entities in total)
• 機能のキーワード: sa239, staphylococcus aureus, ribokinase, transferase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32751.90

構造登録者

Li, J.,Wu, M.,Wang, L.,Zang, J. (登録日: 2011-05-11, 公開日: 2012-04-25, 最終更新日: 2023-11-01)

主引用文献

Li, J.,Wang, C.,Wu, Y.,Wu, M.,Wang, L.,Wang, Y.,Zang, J.
Crystal structure of Sa239 reveals the structural basis for the activation of ribokinase by monovalent cations.
J.Struct.Biol., 177:578-582, 2012

PubMed Abstract: Ribokinase is responsible for catalyzing the reaction of d-ribose and ATP to produce ribose-5-phosphate and ADP, which can be activated by monovalent cations such as potassium, cesium and ammonium. However, the exact activation mechanism of ribokinase remains elusive. Here we report the crystal structure of Sa239, a ribokinase from Staphylococcus aureus, in the absence of monovalent ions. In addition to the dimer form similar to that observed in Escherichia coli ribokinase structure, the structure of Sa239 demonstrates that the C-terminal tail protrudes from the remaining part and interacts with the neighboring molecule, resulting in an unexpected dimerization form. By comparing the structure of Sa239 to E. coli ribokinase, we propose that binding of the monovalent cation triggers the conformational change of the large ATP loop to organize the formation of nucleotide binding pocket, thus enabling ATP binding and enhancing catalytic activity. Our study uncovers the detailed structural basis for the activation mechanism of ribokinase by monovalent cations.

PubMed: 22198595
DOI: 10.1016/j.jsb.2011.12.010

実験手法

X-RAY DIFFRACTION (2.15 Å)