1PKV

The N-terminal domain of riboflavin synthase in complex with riboflavin

1PKV の概要

• エントリーDOI: 10.2210/pdb1pkv/pdb
• 関連するPDBエントリー: 1HZE 1I8D 1KZL
• 分子名称: Riboflavin synthase alpha chain, RIBOFLAVIN (3 entities in total)
• 機能のキーワード: dimer, beta-barrel, greek key motif, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21904.65

構造登録者

Meining, W.,Eberhardt, S.,Bacher, A.,Ladenstein, R. (登録日: 2003-06-06, 公開日: 2004-06-08, 最終更新日: 2023-08-16)

主引用文献

Meining, W.,Eberhardt, S.,Bacher, A.,Ladenstein, R.
The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution.
J.Mol.Biol., 331:1053-1063, 2003

PubMed Abstract: Riboflavin synthase of Escherichia coli is a homotrimer with a molecular mass of 70 kDa. The enzyme catalyzes the dismutation of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine, affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. The N-terminal segment (residues 1-87) and the C-terminal segment (residues 98-187) form beta-barrels with similar fold and a high degree of sequence similarity. A recombinant peptide comprising amino acid residues 1-97 forms a dimer, which binds riboflavin with high affinity. Here, we report the structure of this construct in complex with riboflavin at 2.6A resolution. It is demonstrated that the complex can serve as a model for ligand-binding in the native enzyme. The structure and riboflavin-binding mode is in excellent agreement with structural information obtained from the native enzyme from Escherichia coli and riboflavin synthase from Schizosaccharomyces pombe. The implications for the binding specificity and the regiospecificity of the catalyzed reaction are discussed.

PubMed: 12927541
DOI: 10.1016/S0022-2836(03)00844-1

実験手法

X-RAY DIFFRACTION (2.6 Å)