2vsn | pdb_00002vsn

STRUCTURE AND TOPOLOGICAL ARRANGEMENT OF AN O-GLCNAC TRANSFERASE HOMOLOG: INSIGHT INTO MOLECULAR CONTROL OF INTRACELLULAR GLYCOSYLATION

spinqualitylabelsall models 2vsn, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vsn is a 2 chain structure with sequence from Xanthomonas campestris pv. campestris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: UDP Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous superhelical groove that directs substrates to the active site. Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation.,Martinez-Fleites C, Macauley MS, He Y, Shen DL, Vocadlo DJ, Davies GJ Nat Struct Mol Biol. 2008 Jul;15(7):764-5. Epub 2008 Jun 8. PMID:18536723 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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