3TWO

The crystal structure of CAD from Helicobacter pylori complexed with NADP(H)

3TWO の概要

• エントリーDOI: 10.2210/pdb3two/pdb
• 分子名称: Mannitol dehydrogenase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ZINC ION, ... (4 entities in total)
• 機能のキーワード: helicobacter pylori, cinnamyl-alcohol dehydrogenase, nadp(h), oxidoreductase
• 由来する生物種: Helicobacter pylori
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79225.79

構造登録者

Seo, K.H.,Zhuang, N.N.,Cong, C.,Lee, K.H. (登録日: 2011-09-22, 公開日: 2011-10-12, 最終更新日: 2023-11-01)

主引用文献

Seo, K.H.,Zhuang, N.N.,Chen, C.,Song, J.Y.,Kang, H.L.,Rhee, K.H.,Lee, K.H.
Unusual NADPH conformation in the crystal structure of a cinnamyl alcohol dehydrogenase from Helicobacter pylori in complex with NADP(H) and substrate docking analysis
Febs Lett., 586:337-343, 2012

PubMed Abstract: Cinnamyl alcohol dehydrogenase is a zinc- and NADPH-dependent dehydrogenase catalyzing the reversible conversion of p-hydroxycinnamaldehydes to their corresponding hydroxycinnamyl alcohols. A CAD homolog from Helicobacter pylori (HpCAD) possesses broad substrate specificities like the plant CADs and additionally a dismutation activity converting benzaldehyde to benzyl alcohol and benzoic acid. We have determined the crystal structure of HpCAD complexed with NADP(H) at 2.18Å resolution to get a better understanding of this class of CAD outside of plants. The structure of HpCAD is highly homologous to the sinapyl alcohol dehydrogenase and the plant CAD with well-conserved residues involved in catalysis and zinc binding. However, the NADP(H) binding mode of the HpCAD has been found to be significantly different from those of plant CADs.

PubMed: 22269576
DOI: 10.1016/j.febslet.2012.01.020

実験手法

X-RAY DIFFRACTION (2.18 Å)