2QG6

Crystal structure of human nicotinamide riboside kinase (NRK1) in complex with nicotinamide mononucleotide (NMN)

2QG6 の概要

• エントリーDOI: 10.2210/pdb2qg6/pdb
• 分子名称: Nicotinamide riboside kinase 1, PHOSPHATE ION, BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: nrk, nicotinamide riboside kinase, nad+, nucleoside monophosphate (nmp) kinase, nicotinamide mononucleotide, adp, tiazofurin, signaling protein, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23974.85

構造登録者

Khan, J.A.,Xiang, S.,Tong, L. (登録日: 2007-06-28, 公開日: 2007-10-02, 最終更新日: 2017-10-18)

主引用文献

Khan, J.A.,Xiang, S.,Tong, L.
Crystal structure of human nicotinamide riboside kinase
Structure, 15:1005-1013, 2007

PubMed Abstract: Nicotinamide riboside kinase (NRK) has an important role in the biosynthesis of NAD(+) as well as the activation of tiazofurin and other NR analogs for anticancer therapy. NRK belongs to the deoxynucleoside kinase and nucleoside monophosphate (NMP) kinase superfamily, although the degree of sequence conservation is very low. We report here the crystal structures of human NRK1 in a binary complex with the reaction product nicotinamide mononucleotide (NMN) at 1.5 A resolution and in a ternary complex with ADP and tiazofurin at 2.7 A resolution. The active site is located in a groove between the central parallel beta sheet core and the LID and NMP-binding domains. The hydroxyl groups on the ribose of NR are recognized by Asp56 and Arg129, and Asp36 is the general base of the enzyme. Mutation of residues in the active site can abolish the catalytic activity of the enzyme, confirming the structural observations.

PubMed: 17698003
DOI: 10.1016/j.str.2007.06.017

実験手法

X-RAY DIFFRACTION (1.5 Å)