4ITU

Crystal structure of S-2-HYDROXYPROPYL COENZYME M DEHYDROGENASE (S-HPCDH) bound to S-HPC AND NADH

4ITU の概要

• エントリーDOI: 10.2210/pdb4itu/pdb
• 関連するPDBエントリー: 4GH5
• 分子名称: Short-chain dehydrogenase/reductase SDR, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid, ... (4 entities in total)
• 機能のキーワード: rossmann fold, oxidoreductase
• 由来する生物種: Xanthobacter autotrophicus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 111913.97

構造登録者

Bakelar, J.W.,Johnson, S.J. (登録日: 2013-01-18, 公開日: 2013-03-27, 最終更新日: 2023-09-20)

主引用文献

Bakelar, J.W.,Sliwa, D.A.,Johnson, S.J.
Crystal structures of S-HPCDH reveal determinants of stereospecificity for R- and S-hydroxypropyl-coenzyme M dehydrogenases.
Arch.Biochem.Biophys., 533:62-68, 2013

PubMed Abstract: (R)- and (S)-hydroxypropyl-coenzyme M dehydrogenases (R- and S-HPCDH) are stereospecific enzymes that are central to the metabolism of propylene and epoxide in Xanthobacter autotrophicus. The bacterium produces R- and S-HPCDH simultaneously to facilitate transformation of R- and S-enantiomers of epoxypropane to a common achiral product 2-ketopropyl-CoM (2-KPC). Both R- and S-HPCDH are highly specific for their respective substrates as each enzyme displays less than 0.5% activity with the opposite substrate isomer. In order to elucidate the structural basis for stereospecificity displayed by R- and S-HPCDH we have determined substrate bound crystal structures of S-HPCDH to 1.6Å resolution. Comparisons to the previously reported product-bound structure of R-HPCDH reveal that although the placement of catalytic residues within the active site of each enzyme is nearly identical, structural differences in the surrounding area provide each enzyme with a distinct substrate binding pocket. These structures demonstrate how chiral discrimination by R- and S-HPCDH results from alternative binding of the distal end of substrates within each substrate binding pocket.

PubMed: 23474457
DOI: 10.1016/j.abb.2013.02.017

実験手法

X-RAY DIFFRACTION (1.6 Å)