title: Unusual NADPH conformation in the crystal structure of a cinnamyl alcohol dehydrogenase from Helicobacter pylori in complex with NADP(H) and substrate docking analysis.
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.
authors.affiliation: Division of Applied Life Science (BK21 Program), Gyeongsang National University, Jinju, Republic of Korea.
authors.forename: Kyung Hye
authors.initials: KH
authors.lastname: Seo
authors.forename: Ningning
authors.initials: N
authors.lastname: Zhuang
authors.forename: Cong
authors.initials: C
authors.lastname: Chen
authors.forename: Jae-Young
authors.initials: JY
authors.lastname: Song
authors.forename: Hyung-Lyun
authors.initials: HL
authors.lastname: Kang
authors.forename: Kwang-Ho
authors.initials: KH
authors.lastname: Rhee
authors.forename: Kon Ho
authors.initials: KH
authors.lastname: Lee
mesh_terms: D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004269:DNA, Bacterial / Q000235:genetics; D019281:Dimerization; D016480:Helicobacter pylori / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009243:NAD / Q000737:chemistry; D009249:NADP / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D010940:Plant Proteins; D011994:Recombinant Proteins; D009243:NAD; D009249:NADP; D000429:Alcohol Oxidoreductases; C018656:cinnamyl alcohol dehydrogenase