5zba

Crystal structure of Rtt109-Asf1-H3-H4-CoA complex

spinqualitylabelsall models 5zba, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zba is a 4 chain structure with sequence from Aspergillus fumigatus Af293 and Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Ligands: ALY, COA, IOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4WUS9_ASPFU Publication Abstract from PubMed Rtt109 is a unique histone acetyltransferase acetylating histone H3 lysine 56 (H3K56), a modification critical for DNA replication-coupled nucleosome assembly and genome stability. In cells, histone chaperone Asf1 is essential for H3K56 acetylation, yet the mechanisms for H3K56 specificity and Asf1 requirement remain unknown. We have determined the crystal structure of the Rtt109-Asf1-H3-H4 complex and found that unwinding of histone H3 alphaN, where K56 is normally located, and stabilization of the very C-terminal beta strand of histone H4 by Asf1 are prerequisites for H3K56 acetylation. Unexpectedly, an interaction between Rtt109 and the central helix of histone H3 is also required. The observed multiprotein, multisite substrate recognition mechanism among histone modification enzymes provides mechanistic understandings of Rtt109 and Asf1 in H3K56 acetylation, as well as valuable insights into substrate recognition by histone modification enzymes in general. Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109.,Zhang L, Serra-Cardona A, Zhou H, Wang M, Yang N, Zhang Z, Xu RM Cell. 2018 Aug 9;174(4):818-830.e11. doi: 10.1016/j.cell.2018.07.005. Epub 2018, Jul 26. PMID:30057113 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Anti-silencing factor 3D structures Histone 3D structures

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