2O48

Crystal structure of Mammalian Dimeric Dihydrodiol Dehydrogenase

2O48 の概要

• エントリーDOI: 10.2210/pdb2o48/pdb
• 関連するPDBエントリー: 1OFG 2GLX
• 分子名称: Dimeric dihydrodiol dehydrogenase, SULFATE ION, P-HYDROXYACETOPHENONE, ... (5 entities in total)
• 機能のキーワード: nadp-binding rossmann-fold domain, predominantly anti-parallel beta sheet, oxidoreductase
• 由来する生物種: Macaca fascicularis (crab-eating macaque)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37079.56

構造登録者

Carbone, V.,El-Kabbani, O. (登録日: 2006-12-04, 公開日: 2007-07-31, 最終更新日: 2023-12-27)

主引用文献

Carbone, V.,Endo, S.,Sumii, R.,Chung, R.P.,Matsunaga, T.,Hara, A.,El-Kabbani, O.
Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: probing the subunit interface with site-directed mutagenesis.
Proteins, 70:176-187, 2008

PubMed Abstract: Dimeric dihydrodiol dehydrogenase (DD) catalyses the nicotinamide adenine dinucleotide phosphate (NADP+)-dependent oxidation of trans-dihydrodiols of aromatic hydrocarbons to their corresponding catechols. This is the first report of the crystal structure of the dimeric enzyme determined at 2.0 A resolution. The tertiary structure is formed by a classical dinucleotide binding fold comprising of two betaalphabetaalphabeta motifs at the N-terminus and an eight-stranded, predominantly antiparallel beta-sheet at the C-terminus. The active-site of DD, occupied either by a glycerol molecule or the inhibitor 4-hydroxyacetophenone, is located in the C-terminal domain of the protein and maintained by a number of residues including Lys97, Trp125, Phe154, Leu158, Val161, Asp176, Leu177, Tyr180, Trp254, Phe279, and Asp280. The dimer interface is stabilized by a large number of intermolecular contacts mediated by the beta-sheet of each monomer, which includes an intricate hydrogen bonding network maintained in principal by Arg148 and Arg202. Site-directed mutagenesis has demonstrated that the intact dimer is not essential for catalytic activity. The similarity between the quaternary structures of mammalian DD and glucose-fructose oxidoreductase isolated from the prokaryotic organism Zymomonas mobilis suggests that both enzymes are members of a unique family of oligomeric proteins and may share a common ancestral gene.

PubMed: 17654552
DOI: 10.1002/prot.21566

実験手法

X-RAY DIFFRACTION (2.59 Å)