3jt1

Legionella pneumophila glucosyltransferase Lgt1, UDP-bound form

spinqualitylabelsall models 3jt1, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3jt1 is a 1 chain structure with sequence from Legionella pneumophila str. Lens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: UDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5WWY0_LEGPL Publication Abstract from PubMed The glucosyltransferase Lgt1 is one of three glucosylating toxins of Legionella pneumophila, the causative agent of Legionnaires disease. It acts through specific glucosylation of a serine residue (S53) in the eukaryotic elongation factor 1A and belongs to type A glycosyltransferases. High-resolution crystal structures of Lgt1 show an elongated shape of the protein, with the binding site for uridine disphosphate glucose at the bottom of a deep cleft. Lgt1 shows only a low sequence identity with other type A glycosyltransferases, and structural conservation is limited to a central folding core that is usually observed within this family of proteins. Domains and protrusions added to the core motif represent determinants for the specific recognition and binding of the target. Manual docking experiments based on the crystal structures of toxin and target protein suggest an obvious mode of binding to the target that allows for efficient transfer of a glucose moiety. Structural basis of the action of glucosyltransferase Lgt1 from Legionella pneumophila.,Lu W, Du J, Stahl M, Tzivelekidis T, Belyi Y, Gerhardt S, Aktories K, Einsle O J Mol Biol. 2010 Feb 19;396(2):321-31. Epub 2009 Nov 23. PMID:19941871 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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