3Q9C

Crystal Structure of H159A APAH complexed with N8-acetylspermidine

3Q9C の概要

• エントリーDOI: 10.2210/pdb3q9c/pdb
• 関連するPDBエントリー: 3Q9B 3Q9E 3Q9F
• 分子名称: Acetylpolyamine amidohydrolase, N-{4-[(3-aminopropyl)amino]butyl}acetamide, POTASSIUM ION, ... (6 entities in total)
• 機能のキーワード: hdac, polyamine, arginase fold, deacetylase, hydrolase
• 由来する生物種: Mycoplana ramosa (Mycoplana bullata)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 439412.47

構造登録者

Lombardi, P.M.,Christianson, D.W. (登録日: 2011-01-07, 公開日: 2011-03-02, 最終更新日: 2023-09-13)

主引用文献

Lombardi, P.M.,Angell, H.D.,Whittington, D.A.,Flynn, E.F.,Rajashankar, K.R.,Christianson, D.W.
Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases .
Biochemistry, 50:1808-1817, 2011

PubMed Abstract: Polyamines are a ubiquitous class of polycationic small molecules that can influence gene expression by binding to nucleic acids. Reversible polyamine acetylation regulates nucleic acid binding and is required for normal cell cycle progression and proliferation. Here, we report the structures of Mycoplana ramosa acetylpolyamine amidohydrolase (APAH) complexed with a transition state analogue and a hydroxamate inhibitor and an inactive mutant complexed with two acetylpolyamine substrates. The structure of APAH is the first of a histone deacetylase-like oligomer and reveals that an 18-residue insert in the L2 loop promotes dimerization and the formation of an 18 Å long "L"-shaped active site tunnel at the dimer interface, accessible only to narrow and flexible substrates. The importance of dimerization for polyamine deacetylase function leads to the suggestion that a comparable dimeric or double-domain histone deacetylase could catalyze polyamine deacetylation reactions in eukaryotes.

PubMed: 21268586
DOI: 10.1021/bi101859k

実験手法

X-RAY DIFFRACTION (2.3 Å)