6rhe

CpOGA D298N in complex with hOGA-derived S-GlcNAc peptide

spinqualitylabelsall models 6rhe, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rhe is a 2 chain structure with sequence from Clostridium perfringens ATCC 13124 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: ACE, CD, NAG, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Modification of specific Ser and Thr residues of nucleocytoplasmic proteins with O-GlcNAc, catalyzed by O-GlcNAc transferase (OGT), is an abundant posttranslational event essential for proper animal development and is dysregulated in various diseases. Due to the rapid concurrent removal by the single O-GlcNAcase (OGA), precise functional dissection of site-specific O-GlcNAc modification in vivo is currently not possible without affecting the entire O-GlcNAc proteome. Exploiting the fortuitous promiscuity of OGT, we show that S-GlcNAc is a hydrolytically stable and accurate structural mimic of O-GlcNAc that can be encoded in mammalian systems with CRISPR-Cas9 in an otherwise unperturbed O-GlcNAcome. Using this approach, we target an elusive Ser 405 O-GlcNAc site on OGA, showing that this site-specific modification affects OGA stability. Genetic recoding to dissect the roles of site-specific protein O-GlcNAcylation.,Gorelik A, Bartual SG, Borodkin VS, Varghese J, Ferenbach AT, van Aalten DMF Nat Struct Mol Biol. 2019 Nov;26(11):1071-1077. doi: 10.1038/s41594-019-0325-8., Epub 2019 Nov 6. PMID:31695185 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also O-GlcNAcase

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