6RXJ
Crystal structure of CobB wt in complex with H4K16-Acetyl peptide
Summary for 6RXJ
| Entry DOI | 10.2210/pdb6rxj/pdb |
| Descriptor | NAD-dependent protein deacylase, Histone H4, ZINC ION, ... (4 entities in total) |
| Functional Keywords | deacylase, nad-dependent, acetyl, lysine, ptm, hydrolase |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 4 |
| Total formula weight | 58739.23 |
| Authors | Spinck, M.,Gasper, R.,Neumann, H. (deposition date: 2019-06-08, release date: 2020-04-15, Last modification date: 2024-10-23) |
| Primary citation | Spinck, M.,Neumann-Staubitz, P.,Ecke, M.,Gasper, R.,Neumann, H. Evolved, Selective Erasers of Distinct Lysine Acylations. Angew.Chem.Int.Ed.Engl., 59:11142-11149, 2020 Cited by PubMed Abstract: Lysine acylations, a family of diverse protein modifications varying in acyl-group length, charge, and saturation, are linked to many important physiological processes. Only a small set of substrate-promiscuous lysine acetyltransferases and deacetylases (KDACs) install and remove this vast variety of modifications. Engineered KDACs that remove only one type of acylation would help to dissect the different contributions of distinct acylations. We developed a bacterial selection system for the directed evolution of KDACs and identified variants up to 400 times more selective for butyryl-lysine compared to crotonyl-lysine. Structural analyses revealed that the enzyme adopts different conformational states depending on the type of acylation of the bound peptide. We used the butyryl-selective KDAC variant to shift the cellular acylation spectrum towards increased lysine crotonylation. These new enzymes will help in dissecting the roles of different lysine acylations in cell physiology. PubMed: 32187803DOI: 10.1002/anie.202002899 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
