3zj0

The human O-GlcNAcase C-terminal domain is a pseudo histone acetyltransferase

spinqualitylabelsall models 3zj0, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zj0 is a 1 chain structure with sequence from Oceanicola granulosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: ACO, CL, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AT_OCEGH Binds acetyl-CoA, but not butyryl-CoA or decanoyl-CoA. May have acetyltransferase activity. Publication Abstract from PubMed The dynamic modification of proteins by O-linked N-acetylglucosamine (O-GlcNAc) is an essential posttranslational modification present in higher eukaryotes. Removal of O-GlcNAc is catalysed by O-GlcNAcase, a multi-domain enzyme that has been reported to be bifunctional, possessing both glycoside hydrolase and histone acetyltransferase (AT) activity. Insights into the mechanism, protein substrate recognition and inhibition of the hydrolase domain of human OGA (hOGA) have been obtained via the use of the structures of bacterial homologues. However, the molecular basis of AT activity of OGA, which has only been reported in vitro, is not presently understood. Here, we describe the crystal structure of a putative acetyltransferase (OgpAT) that we identified in the genome of the marine bacterium Oceanicola granulosus, showing homology to the hOGA C-terminal AT domain (hOGA-AT). The structure of OgpAT in complex with acetyl coenzyme A (AcCoA) reveals that, by homology modelling, hOGA-AT adopts a variant AT fold with a unique loop creating a deep tunnel. The structures, together with mutagenesis and surface plasmon resonance data, reveal that while the bacterial OgpAT binds AcCoA, the hOGA-AT does not, as explained by the lack of key residues normally required to bind AcCoA. Thus, the C-terminal domain of hOGA is a catalytically incompetent 'pseudo'-AT. Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain.,Rao FV, Schuttelkopf AW, Dorfmueller HC, Ferenbach AT, Navratilova I, van Aalten DM Open Biol. 2013 Oct 2;3(10):130021. PMID:24088714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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