1RHC

F420-dependent secondary alcohol dehydrogenase in complex with an F420-acetone adduct

1RHC の概要

• エントリーDOI: 10.2210/pdb1rhc/pdb
• 分子名称: F420-dependent alcohol dehydrogenase, CHLORIDE ION, POTASSIUM ION, ... (6 entities in total)
• 機能のキーワード: (alpha, beta)8 barrel, oxidoreductase
• 由来する生物種: Methanoculleus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38141.29

構造登録者

Aufhammer, S.W.,Warkentin, E.,Berk, H.,Shima, S.,Thauer, R.K.,Ermler, U. (登録日: 2003-11-14, 公開日: 2004-03-30, 最終更新日: 2024-02-14)

主引用文献

Aufhammer, S.W.,Warkentin, E.,Berk, H.,Shima, S.,Thauer, R.K.,Ermler, U.
Coenzyme binding in f(420)-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family.
Structure, 12:361-370, 2004

PubMed Abstract: F(420)-dependent secondary alcohol dehydrogenase (Adf) from methanogenic archaea is a member of the growing bacterial luciferase family which are all TIM barrel enzymes, most of which with an unusual nonprolyl cis peptide bond. We report here on the crystal structure of Adf from Methanoculleus thermophilicus at 1.8 A resolution in complex with a F(420)-acetone adduct. The knowledge of the F(420) binding mode in Adf provides the molecular basis for modeling F(420) and FMN into the other enzymes of the family. A nonprolyl cis peptide bond was identified as an essential part of a bulge that serves as backstop at the Re-face of F(420) to keep it in a bent conformation. The acetone moiety of the F(420)-acetone adduct is positioned at the Si-face of F(420) deeply buried inside the protein. Isopropanol can be reliably modeled and a hydrogen transfer mechanism postulated. His39 and Glu108 can be identified as key players for binding of the acetone or isopropanol oxygens and for catalysis.

PubMed: 15016352
DOI: 10.1016/j.str.2004.02.010

実験手法

X-RAY DIFFRACTION (1.8 Å)