2VRC

Crystal structure of the Citrobacter sp. triphenylmethane reductase complexed with NADP(H)

2VRC の概要

• エントリーDOI: 10.2210/pdb2vrc/pdb
• 関連するPDBエントリー: 2VRB
• 分子名称: TRIPHENYLMETHANE REDUCTASE (3 entities in total)
• 機能のキーワード: reductase, sdr family, oxidoreductase, triphenylmethane reduction
• 由来する生物種: CITROBACTER SP. MY-5; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 124194.24

構造登録者

Kim, Y.,Park, H.J.,Kwak, S.N.,Lee, J.S.,Oh, T.K.,Kim, M.H. (登録日: 2008-03-31, 公開日: 2008-09-23, 最終更新日: 2024-11-13)

主引用文献

Kim, M.H.,Kim, Y.,Park, H.J.,Lee, J.S.,Kwak, S.N.,Jung, W.H.,Lee, S.G.,Kim, D.,Lee, Y.C.,Oh, T.K.
Structural Insight Into Bioremediation of Triphenylmethane Dyes by Citrobacter Sp. Triphenylmethane Reductase.
J.Biol.Chem., 283:31981-, 2008

PubMed Abstract: Triphenylmethane dyes are aromatic xenobiotic compounds that are widely considered to be one of the main culprits of environmental pollution. Triphenylmethane reductase (TMR) from Citrobacter sp. strain KCTC 18061P was initially isolated and biochemically characterized as an enzyme that catalyzes the reduction of triphenylmethane dyes. Information from the primary amino acid sequence suggests that TMR is a dinucleotide-binding motif-containing enzyme; however, no other functional clues can be derived from sequence analysis. We present the crystal structure of TMR in complex with NADP+ at 2.0-angstroms resolution. Despite limited sequence similarity, the enzyme shows remarkable structural similarity to short-chain dehydrogenase/reductase (SDR) family proteins. Functional assignments revealed that TMR has features of both classic and extended SDR family members and does not contain a conserved active site. Thus, it constitutes a novel class of SDR family proteins. On the basis of simulated molecular docking using the substrate malachite green and the TMR/NADP+ crystal structure, together with site-directed mutagenesis, we have elucidated a potential molecular mechanism for triphenylmethane dye reduction.

PubMed: 18782772
DOI: 10.1074/JBC.M804092200

実験手法

X-RAY DIFFRACTION (2.5 Å)