In this section
@article{Campeotto:2014:10.1074/jbc.M114.590570,
author = {Campeotto, I and Percy, MG and MacDonald, JT and Foerster, A and Freemont, PS and Gruendling, A},
doi = {10.1074/jbc.M114.590570},
journal = {Journal of Biological Chemistry},
pages = {28054--28069},
title = {Structural and Mechanistic Insight into the Listeria monocytogenes Two-enzyme Lipoteichoic Acid Synthesis System},
url = {http://dx.doi.org/10.1074/jbc.M114.590570},
volume = {289},
year = {2014}
}
TY - JOUR
AB - Lipoteichoic acid (LTA) is an important cell wall componentrequired for proper cell growth in many Gram-positive bacteria.In Listeria monocytogenes, two enzymes are required for the synthesisof this polyglycerolphosphate polymer. The LTA primaseLtaPLm initiates LTA synthesis by transferring the first glycerolphosphate(GroP) subunit onto the glycolipid anchor and theLTA synthase LtaSLm extends the polymer by the repeated additionof GroP subunits to the tip of the growing chain. Here, wepresent the crystal structures of the enzymatic domains ofLtaPLm and LtaSLm. Although the enzymes share the same fold,substantial differences in the cavity of the catalytic site andsurface charge distribution contribute to enzyme specialization.The eLtaSLm structure was also determined in complexwith GroP revealing a second GroP binding site. Mutationalanalysis confirmed an essential function for this binding siteand allowed us to propose a model for the binding of thegrowing chain.
AU - Campeotto,I
AU - Percy,MG
AU - MacDonald,JT
AU - Foerster,A
AU - Freemont,PS
AU - Gruendling,A
DO - 10.1074/jbc.M114.590570
EP - 28069
PY - 2014///
SN - 0021-9258
SP - 28054
TI - Structural and Mechanistic Insight into the Listeria monocytogenes Two-enzyme Lipoteichoic Acid Synthesis System
T2 - Journal of Biological Chemistry
UR - http://dx.doi.org/10.1074/jbc.M114.590570
UR - http://hdl.handle.net/10044/1/55958
VL - 289
ER -
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