5LKT
Crystal structure of the p300 acetyltransferase catalytic core with butyryl-coenzyme A.
Summary for 5LKT
| Entry DOI | 10.2210/pdb5lkt/pdb |
| Related | 4BHW |
| Descriptor | Histone acetyltransferase p300,Histone acetyltransferase p300, ZINC ION, Butyryl Coenzyme A, ... (7 entities in total) |
| Functional Keywords | p300 acetyltransferase, butyryl-coa, chromatin modification, acylation, transferase |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Cytoplasm: Q09472 |
| Total number of polymer chains | 1 |
| Total formula weight | 68591.82 |
| Authors | Kaczmarska, Z.,Ortega, E.,Marquez, J.A.,Panne, D. (deposition date: 2016-07-24, release date: 2016-11-02, Last modification date: 2024-01-10) |
| Primary citation | Kaczmarska, Z.,Ortega, E.,Goudarzi, A.,Huang, H.,Kim, S.,Marquez, J.A.,Zhao, Y.,Khochbin, S.,Panne, D. Structure of p300 in complex with acyl-CoA variants. Nat. Chem. Biol., 13:21-29, 2017 Cited by PubMed Abstract: Histone acetylation plays an important role in transcriptional activation. Histones are also modified by chemically diverse acylations that are frequently deposited by p300, a transcriptional coactivator that uses a number of different acyl-CoA cofactors. Here we report that while p300 is a robust acetylase, its activity gets weaker with increasing acyl-CoA chain length. Crystal structures of p300 in complex with propionyl-, crotonyl-, or butyryl-CoA show that the aliphatic portions of these cofactors are bound in the lysine substrate-binding tunnel in a conformation that is incompatible with substrate transfer. Lysine substrate binding is predicted to remodel the acyl-CoA ligands into a conformation compatible with acyl-chain transfer. This remodeling requires that the aliphatic portion of acyl-CoA be accommodated in a hydrophobic pocket in the enzymes active site. The size of the pocket and its aliphatic nature exclude long-chain and charged acyl-CoA variants, presumably explaining the cofactor preference for p300. PubMed: 27820805DOI: 10.1038/nchembio.2217 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.04 Å) |
Structure validation
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