3TWO
The crystal structure of CAD from Helicobacter pylori complexed with NADP(H)
Summary for 3TWO
| Entry DOI | 10.2210/pdb3two/pdb |
| Descriptor | Mannitol dehydrogenase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ZINC ION, ... (4 entities in total) |
| Functional Keywords | helicobacter pylori, cinnamyl-alcohol dehydrogenase, nadp(h), oxidoreductase |
| Biological source | Helicobacter pylori |
| Total number of polymer chains | 2 |
| Total formula weight | 79225.79 |
| Authors | Seo, K.H.,Zhuang, N.N.,Cong, C.,Lee, K.H. (deposition date: 2011-09-22, release date: 2011-10-12, Last modification date: 2023-11-01) |
| Primary citation | 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 Cited by 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: 22269576DOI: 10.1016/j.febslet.2012.01.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.18 Å) |
Structure validation
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