1NB0

Crystal Structure of Human Riboflavin Kinase

1NB0 の概要

• エントリーDOI: 10.2210/pdb1nb0/pdb
• 関連するPDBエントリー: 1nb9 1nbg
• 分子名称: hypothetical protein FLJ11149, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: beta barrel, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): Q969G6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17223.59

構造登録者

Karthikeyan, S.,Zhou, Q.,Mseeh, F.,Grishin, N.V.,Osterman, A.L.,Zhang, H. (登録日: 2002-12-01, 公開日: 2003-03-11, 最終更新日: 2024-02-14)

主引用文献

Karthikeyan, S.,Zhou, Q.,Mseeh, F.,Grishin, N.V.,Osterman, A.L.,Zhang, H.
Crystal Structure of Human Riboflavin Kinase Reveals a Beta Barrel Fold and a Novel Active Site Arch
Structure, 11:265-273, 2003

PubMed Abstract: Riboflavin kinase (RFK) is an essential enzyme catalyzing the phosphorylation of riboflavin (vitamin B(2)) to form FMN, an obligatory step in vitamin B(2) utilization and flavin cofactor synthesis. The structure of human RFK revealed a six-stranded antiparallel beta barrel core structurally similar to the riboflavin synthase/ferredoxin reductase FAD binding domain fold. The binding site of an intrinsically bound MgADP defines a novel nucleotide binding motif that encompasses a loop, a 3(10) helix, and a reverse turn followed by a short beta strand. This active site loop forms an arch with ATP and riboflavin binding at the opposite side and the phosphoryl transfer appears to occur through the hole underneath the arch. The invariant residues Asn36 and Glu86 are implicated in the catalysis.

PubMed: 12623014
DOI: 10.1016/S0969-2126(03)00024-8

実験手法

X-RAY DIFFRACTION (1.7 Å)