6rxj

Crystal structure of CobB wt in complex with H4K16-Acetyl peptide

spinqualitylabelsall models 6rxj, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: ALY, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 to cell physiology. Therefore, we developed a bacterial selection system for the directed evolution of KDACs with which we identified variants up to 400 times more selective for butyryl- 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. Hence, these new enzymes will help dissecting the different roles of lysine acylations in cell physiology. Evolved, Selective Erasers of Distinct Lysine Acylations.,Spinck M, Neumann-Staubitz P, Ecke M, Gasper R, Neumann H Angew Chem Int Ed Engl. 2020 Mar 18. doi: 10.1002/anie.202002899. PMID:32187803 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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