2w5s

Structure-based mechanism of lipoteichoic acid synthesis by Staphylococcus aureus LtaS.

spinqualitylabelsall models 2w5s, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w5s is a 1 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, GP9, MN Related: 2w5t, 2w5r, 2w5q Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LTAS_STAAW] Catalyzes the polymerization of lipoteichoic acid (LTA) polyglycerol phosphate, a reaction that presumably uses phosphatidylglycerol (PG) as substrate. Is required for staphylococcal growth and cell division process (By similarity). 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 Staphylococcus aureus synthesizes polyglycerol-phosphate lipoteichoic acid (LTA) from phosphatidylglycerol. LtaS, a predicted membrane protein with 5 N-terminal transmembrane helices followed by a large extracellular part (eLtaS), is required for staphylococcal growth and LTA synthesis. Here, we report the first crystal structure of the eLtaS domain at 1.2-A resolution and show that it assumes a sulfatase-like fold with an alpha/beta core and a C-terminal part composed of 4 anti-parallel beta-strands and a long alpha-helix. Overlaying eLtaS with sulfatase structures identified active site residues, which were confirmed by alanine substitution mutagenesis and in vivo enzyme function assays. The cocrystal structure with glycerol-phosphate and the coordination of a Mn(2+) cation allowed us to propose a reaction mechanism, whereby the active site threonine of LtaS functions as nucleophile for phosphatidylglycerol hydrolysis and formation of a covalent threonine-glycerolphosphate intermediate. These results will aid in the development of LtaS-specific inhibitors for S. aureus and many other Gram-positive pathogens. Structure-based mechanism of lipoteichoic acid synthesis by Staphylococcus aureus LtaS.,Lu D, Wormann ME, Zhang X, Schneewind O, Grundling A, Freemont PS Proc Natl Acad Sci U S A. 2009 Jan 23. PMID:19168632 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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