3qm0 | pdb_00003qm0

Crystal structure of RTT109-AC-CoA complex

spinqualitylabelsall models 3qm0, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qm0 is a 1 chain structure with sequence from Atcc 18824. This structure supersedes the now removed PDB entry 3d35. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACO, HG NonStd Res: ALY Gene: KIM2, L1377, REM50, RTT109, YLL002W (ATCC 18824) Activity: Histone acetyltransferase, with EC number 2.3.1.48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RT109_YEAST] Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G(2)/M phase of the cell cycle and is involved in transcription DNA repair process. H3K56 acetylation weakens of the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly. Involved in regulation of Ty1 transposition. Publication Abstract from PubMed Rtt109, also known as KAT11, is a recently characterized fungal-specific histone acetyltransferase (HAT) that modifies histone H3 lysine 56 (H3K56) to promote genome stability. Rtt109 does not show sequence conservation with other known HATs and depends on association with either of two histone chaperones, Asf1 or Vps75, for HAT activity. Here we report the X-ray crystal structure of an Rtt109-acetyl coenzyme A complex and carry out structure-based mutagenesis, combined with in vitro biochemical studies of the Rtt109-Vps75 complex and studies of Rtt109 function in vivo. The Rtt109 structure reveals noteworthy homology to the metazoan p300/CBP HAT domain but exhibits functional divergence, including atypical catalytic properties and mode of cofactor regulation. The structure reveals a buried autoacetylated lysine residue that we show is also acetylated in the Rtt109 protein purified from yeast cells. Implications for understanding histone substrate and chaperone binding by Rtt109 are discussed. Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP.,Tang Y, Holbert MA, Wurtele H, Meeth K, Rocha W, Gharib M, Jiang E, Thibault P, Verreault A, Cole PA, Marmorstein R Nat Struct Mol Biol. 2008 Jul;15(7):738-45. Epub 2008 Jun 22. PMID:18568037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone acetyltransferase 3D structures

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