5G11

Pseudomonas aeruginosa HDAH bound to PFSAHA.

5G11 の概要

• エントリーDOI: 10.2210/pdb5g11/pdb
• 関連するPDBエントリー: 5G0X 5G0Y 5G10 5G12 5G13 5G14 5G17
• 分子名称: HDAH, 2,2,3,3,4,4,5,5,6,6,7,7-dodecakis(fluoranyl)-~{N}-oxidanyl-~{N}'-phenyl-octanediamide, ZINC ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, hdah, hdac, hdlp
• 由来する生物種: PSEUDOMONAS AERUGINOSA
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83150.11

構造登録者

Kraemer, A.,Meyer-Almes, F.J.,Yildiz, O. (登録日: 2016-03-23, 公開日: 2016-11-30, 最終更新日: 2024-01-10)

主引用文献

Kramer, A.,Wagner, T.,Yildiz, O.,Meyer-Almes, F.J.
Crystal Structure of a Histone Deacetylase Homologue from Pseudomonas aeruginosa.
Biochemistry, 55:6858-6868, 2016

PubMed Abstract: Despite the recently growing interest in the acetylation of lysine residues by prokaryotic enzymes, the underlying biological function is still not well understood. Deacetylation is accomplished by proteins that belong to the histone deacetylase (HDAC) superfamily. In this report, we present the first crystal structure of PA3774, a histone deacetylase homologue from the human pathogen Pseudomonas aeruginosa that shares a high degree of homology with class IIb HDACs. We determined the crystal structure of the ligand-free enzyme and protein-ligand complexes with a trifluoromethylketone inhibitor and the reaction product acetate. Moreover, we produced loss of function mutants and determined the structure of the inhibitor-free PA3774 mutant, the inhibitor-free PA3774 mutant, and the PA3774 mutant in complex with the highly selective hydroxamate inhibitor PFSAHA. The overall structure reveals that the exceptionally long L1 loop mediates the formation of a tetramer composed of two "head-to-head" dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity.

PubMed: 27951649
DOI: 10.1021/acs.biochem.6b00613

実験手法

X-RAY DIFFRACTION (2.48 Å)