4UOP

Crystal structure of the lipoteichoic acid synthase LtaP from Listeria monocytogenes

Summary for 4UOP

• Entry DOI: 10.2210/pdb4uop/pdb
• Related: 4UOO 4UOR
• Descriptor: LIPOTEICHOIC ACID PRIMASE, PENTAETHYLENE GLYCOL, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: transferase, gram positive, cell wall
• Biological source: LISTERIA MONOCYTOGENES
• Total number of polymer chains: 2
• Total formula weight: 102229.42

Authors

Campeotto, I.,Freemont, P.,Grundling, A. (deposition date: 2014-06-06, release date: 2014-08-27, Last modification date: 2024-01-10)

Primary citation

Campeotto, I.,Percy, M.G.,MacDonald, J.T.,Forster, A.,Freemont, P.S.,Grundling, A.
Structural and mechanistic insight into the Listeria monocytogenes two-enzyme lipoteichoic acid synthesis system.
J. Biol. Chem., 289:28054-28069, 2014

PubMed 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 LtaP(Lm) initiates LTA synthesis by transferring the first glycerolphosphate (GroP) subunit onto the glycolipid anchor and the LTA synthase LtaS(Lm) 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 LtaP(Lm) and LtaS(Lm). 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 eLtaS(Lm) 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.

PubMed: 25128528
DOI: 10.1074/jbc.M114.590570

Experimental method

X-RAY DIFFRACTION (1.75 Å)