3PND

FAD binding by ApbE protein from Salmonella enterica: a new class of FAD binding proteins

3PND の概要

• エントリーDOI: 10.2210/pdb3pnd/pdb
• 関連するPDBエントリー: 1VRM 2O18
• 分子名称: Thiamine biosynthesis lipoprotein ApbE, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: apbe, fad, flavoprotein, oxidoreductase, fad binding domain, t-fold, protein binding
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium
• 細胞内の位置: Cell membrane; Lipid-anchor (Potential): P41780
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 155312.08

構造登録者

Boyd, J.M.,Endrizzi, J.A.,Hamilton, T.L.,Christopherson, M.R.,Mulder, D.W.,Downs, D.M.,Peters, J.W. (登録日: 2010-11-18, 公開日: 2011-01-05, 最終更新日: 2023-09-06)

主引用文献

Boyd, J.M.,Endrizzi, J.A.,Hamilton, T.L.,Christopherson, M.R.,Mulder, D.W.,Downs, D.M.,Peters, J.W.
FAD binding by ApbE protein from Salmonella enterica: a new class of FAD-binding proteins.
J.Bacteriol., 193:887-895, 2011

PubMed Abstract: The periplasmic protein ApbE was identified through the analysis of several mutants defective in thiamine biosynthesis and was implicated as having a role in iron-sulfur cluster biosynthesis or repair. While mutations in apbE cause decreased activity of several iron-sulfur enzymes in vivo, the specific role of ApbE remains unknown. Members of the AbpE family include NosX and RnfF, which have been implicated in oxidation-reduction associated with nitrous oxide and nitrogen metabolism, respectively. In this work, we show that ApbE binds one FAD molecule per monomeric unit. The structure of ApbE in the presence of bound FAD reveals a new FAD-binding motif. Protein variants that are nonfunctional in vivo were generated by random and targeted mutagenesis. Each variant was substituted in the environment of the FAD and analyzed for FAD binding after reconstitution. The variant that altered a key tyrosine residue involved in FAD binding prevented reconstitution of the protein.

PubMed: 21148731
DOI: 10.1128/JB.00730-10

実験手法

X-RAY DIFFRACTION (2.75 Å)