4uop

Crystal structure of the lipoteichoic acid synthase LtaP from Listeria monocytogenes

spinqualitylabelsall models 4uop, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uop is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, CL, MG Related: 4uoo, 4uor Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Lipoteichoic acid (LTA) is an important cell wall component required for proper cell growth in many Gram-positive bacteria. In Listeria monocytogenes, two enzymes are required for the synthesis of this polyglycerolphosphate polymer. The LTA primase LtaPLm initiates LTA synthesis by transferring the first glycerolphosphate (GroP) subunit onto the glycolipid anchor and the LTA synthase LtaSLm extends the polymer by the repeated addition of GroP subunits to the tip of the growing chain. Here, we present the crystal structures of the enzymatic domains of LtaPLm and LtaSLm. While the enzymes share the same fold, substantial differences in the cavity of the catalytic site and surface charge distribution contribute to enzyme specialization. The eLtaSLm structure was also determined in complex with GroP revealing a second GroP binding site. Mutational analysis confirmed an essential function for this binding site and allowed us to propose a model for the binding of the growing chain. Structural and Mechanistic Insight into the Listeria monocytogenes Two-Enzyme Lipoteichoic Acid Synthesis System.,Campeotto I, Percy MG, MacDonald JT, Forster A, Freemont PS, Grundling A J Biol Chem. 2014 Aug 15. pii: jbc.M114.590570. PMID:25128528 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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