4B4W

Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor and an inhibitor

4B4W の概要

• エントリーDOI: 10.2210/pdb4b4w/pdb
• 関連するPDBエントリー: 4B4U 4B4V
• 分子名称: BIFUNCTIONAL PROTEIN FOLD, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: ACINETOBACTER BAUMANNII ATCC 19606
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66865.22

構造登録者

Eadsforth, T.C.,Maluf, F.V.,Hunter, W.N. (登録日: 2012-08-01, 公開日: 2012-08-22, 最終更新日: 2023-12-20)

主引用文献

Eadsforth, T.C.,Maluf, F.V.,Hunter, W.N.
Acinetobacter Baumannii Fold Ligand Complexes; Potent Inhibitors of Folate Metabolism and a Re-Evaluation of the Ly374571 Structure.
FEBS J., 279:4350-, 2012

PubMed Abstract: The bifunctional N(5),N(10)-methylenetetrahydrofolate dehydrogenase/cyclohydrolase (DHCH or FolD), which is widely distributed in prokaryotes and eukaryotes, is involved in the biosynthesis of folate cofactors that are essential for growth and cellular development. The enzyme activities represent a potential antimicrobial drug target. We have characterized the kinetic properties of FolD from the Gram-negative pathogen Acinetobacter baumanni and determined high-resolution crystal structures of complexes with a cofactor and two potent inhibitors. The data reveal new details with respect to the molecular basis of catalysis and potent inhibition. A unexpected finding was that our crystallographic data revealed a different structure for LY374571 (an inhibitor studied as an antifolate) than that previously published. The implications of this observation are discussed.

PubMed: 23050773
DOI: 10.1111/FEBS.12025

実験手法

X-RAY DIFFRACTION (2 Å)