4u9v

Crystal structure of NatD (Naa40p) bound to acetyl CoA

spinqualitylabelsall models 4u9v, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4u9v is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.78Å Ligands: ACO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NAA40_HUMAN Responsible for the acetylation of the N-terminal residues of histones H4 and H2A. Publication Abstract from PubMed N-terminal acetylation is among the most common protein modifications in eukaryotes and is mediated by evolutionarily conserved N-terminal acetyltransferases (NATs). NatD is among the most selective NATs; its only known substrates are histones H4 and H2A, containing the N-terminal sequence SGRGK in humans. Here we characterize the molecular basis for substrate-specific acetylation by NatD by reporting its crystal structure bound to cognate substrates and performing related biochemical studies. A novel N-terminal segment wraps around the catalytic core domain to make stabilizing interactions, and the alpha1-alpha2 and beta6-beta7 loops adopt novel conformations to properly orient the histone N termini in the binding site. Ser1 and Arg3 of the histone make extensive contacts to highly conserved NatD residues in the substrate binding pocket, and flanking glycine residues also appear to contribute to substrate-specific binding by NatD, together defining a Ser-Gly-Arg-Gly recognition sequence. These studies have implications for understanding substrate-specific acetylation by NAT enzymes. The Molecular Basis for Histone H4- and H2A-Specific Amino-Terminal Acetylation by NatD.,Magin RS, Liszczak GP, Marmorstein R Structure. 2015 Feb 3;23(2):332-41. doi: 10.1016/j.str.2014.10.025. Epub 2015 Jan, 22. PMID:25619998 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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