3mgb | pdb_00003mgb

Teg 12 Ternary Structure Complexed with PAP and the Teicoplanin Aglycone

spinqualitylabelsall models 3mgb, resolution 2.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3mgb is a 4 chain structure with sequence from Nonomuraea gerenzanensis and Uncultured soil bacterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.04Å Ligands: 3FG, 3MY, ACT, CL, GHP, OMY, PAP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7T1D7_9BACT 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 The TEG gene cluster, a glycopeptide biosynthetic gene cluster that is predicted to encode the biosynthesis of a polysulfated glycopeptide congener, was recently cloned from DNA extracted directly from desert soil. This predicted glycopeptide gene cluster contains three closely related sulfotransferases (Teg12, -13, and -14) that sulfate teicoplanin-like glycopeptides at three unique sites. Here we report a series of structures: an apo structure of Teg12, Teg12 bound to the desulfated cosubstrate 3'-phosphoadenosine 5'-phosphate, and Teg12 bound to the teicoplanin aglycone. Teg12 appears to undergo a series of significant conformational rearrangements during glycopeptide recruitment, binding, and catalysis. Loop regions that exhibit the most conformational flexibility show the least sequence conservation between TEG sulfotransferases. Site-directed mutagenesis guided by our structural studies confirmed the importance of key catalytic residues as well as the importance of residues found throughout the conformationally flexible loop regions. Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone.,Bick MJ, Banik JJ, Darst SA, Brady SF Biochemistry. 2010 May 18;49(19):4159-68. PMID:20361791 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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