2xsa | pdb_00002xsa

OgOGA apostructure

spinqualitylabelsall models 2xsa, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xsa is a 1 chain structure with sequence from Ocegh. The September 2011 RCSB PDB Molecule of the Month feature on O-GlcNAc Transferase by David Goodsell is 10.2210/rcsb_pdb/mom_2011_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL Related: 2xsb Activity: Beta-N-acetylhexosaminidase, with EC number 3.2.1.52 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q2CEE3_OCEGH] Cleaves GlcNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrate (in vitro). Publication Abstract from PubMed Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes. O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or beta-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms. In the present study, we uncovered the first insights into the mechanism of substrate recognition by human OGA. The structure of a novel bacterial OGA orthologue reveals a putative substrate-binding groove, conserved in metazoan OGAs. Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-beta-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay. The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins. Human OGA binds substrates in a conserved peptide recognition groove.,Schimpl M, Schuttelkopf AW, Borodkin VS, van Aalten DM Biochem J. 2010 Oct 25;432(1):1-7. PMID:20863279 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also O-GlcNAcase

Proteopedia Page Contributors and Editors (what is this?)

OCA