1RAL

THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3ALPHA-HYDROXYSTEROID(SLASH)DIHYDRODIOL DEHYDROGENASE: A MEMBER OF THE ALDO-KETO REDUCTASE SUPERFAMILY

1RAL の概要

• エントリーDOI: 10.2210/pdb1ral/pdb
• 分子名称: 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE (1 entity in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm: P23457
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35331.75

構造登録者

Hoog, S.S.,Pawlowski, J.E.,Alzari, P.M.,Penning, T.M.,Lewis, M. (登録日: 1994-02-04, 公開日: 1994-04-30, 最終更新日: 2024-02-14)

主引用文献

Hoog, S.S.,Pawlowski, J.E.,Alzari, P.M.,Penning, T.M.,Lewis, M.
Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily.
Proc.Natl.Acad.Sci.USA, 91:2517-2521, 1994

PubMed Abstract: The 3.0-A-resolution x-ray structure of rat liver 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase (3 alpha-HSD, EC 1.1.1.50) was determined by molecular replacement using human placental aldose reductase as the search model. The protein folds into an alpha/beta or triose-phosphate isomerase barrel and lacks a canonical Rossmann fold for binding pyridine nucleotide. The structure contains a concentration of hydrophobic amino acids that lie in a cavity near the top of the barrel and that are presumed to be involved in binding hydrophobic substrates (steroids, prostaglandins, and polycyclic aromatic hydrocarbons) and inhibitors (nonsteroidal antiinflammatory drugs). At the distal end of this cavity lie three residues in close proximity that have been implicated in catalysis by site-directed mutagenesis--Tyr-55, Asp-50, and Lys-84. Tyr-55 is postulated to act as the general acid. 3 alpha-HSD shares significant sequence identity with other HSDs that belong to the aldo-keto reductase superfamily and these may show similar architecture. Other members of this family include prostaglandin F synthase and rho-crystallin. By contrast, 3 alpha-HSD shares no sequence identity with HSDs that are members of the short-chain alcohol dehydrogenase family but does contain the Tyr-Xaa-Xaa-Xaa-Lys consensus sequence implicated in catalysis in this family. In the 3 alpha-HSD structure these residues are on the periphery of the barrel and are unlikely to participate in catalysis.

PubMed: 8146147
DOI: 10.1073/pnas.91.7.2517

実験手法

X-RAY DIFFRACTION (3 Å)