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Structural and Mechanistic Insight into the Listeria monocytogenes Two-Enzyme Lipoteichoic Acid Synthesis System

DOI: 10.1074/jbc.M114.590570 DOI Help
PMID: 25128528 PMID Help

Authors: Ivan Campeotto (Imperial College London) , Matthew G. Percy (Imperial College London) , James Macdonald (Imperial College London) , Andreas Forster (Imperial College London) , Paul Freemont (Imperial College London) , Angelika Gr√ľndling (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry

State: Published (Approved)
Published: August 2014
Diamond Proposal Number(s): 6384 , 7299

Open Access Open Access

Abstract: 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. Although 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.

Journal Keywords: Lta Synthesis; Protein Structure; Enzyme Function; Cell Wall; Bacteria; Lipid

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography

Other Facilities: PROXIMA1 (SOLEIL synchrotron, Paris, France)