5G11
Pseudomonas aeruginosa HDAH bound to PFSAHA.
Summary for 5G11
| Entry DOI | 10.2210/pdb5g11/pdb |
| Related | 5G0X 5G0Y 5G10 5G12 5G13 5G14 5G17 |
| Descriptor | 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) |
| Functional Keywords | hydrolase, hdah, hdac, hdlp |
| Biological source | PSEUDOMONAS AERUGINOSA |
| Total number of polymer chains | 2 |
| Total formula weight | 83150.11 |
| Authors | Kraemer, A.,Meyer-Almes, F.J.,Yildiz, O. (deposition date: 2016-03-23, release date: 2016-11-30, Last modification date: 2024-01-10) |
| Primary citation | 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 Cited by 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: 27951649DOI: 10.1021/acs.biochem.6b00613 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.48 Å) |
Structure validation
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