Structural and Mechanistic Insight into the Listeria monocytogenes Two-enzyme Lipoteichoic Acid Synthesis System
Author(s)
Type
Journal Article
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.
Date Issued
2014-10-10
Date Acceptance
2014-08-12
ISSN
0021-9258
Publisher
American Society for Biochemistry and Molecular Biology
Start Page
28054
End Page
28069
Journal / Book Title
Journal of Biological Chemistry
Volume
289
Issue
41
Copyright Statement
© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
Author's Choice—Final version full access.
Creative Commons Attribution Unported License applies to Author Choice Articles
Author's Choice—Final version full access.
Creative Commons Attribution Unported License applies to Author Choice Articles
Sponsor
Medical Research Council (MRC)
Medical Research Council (MRC)
Commission of the European Communities
Grant Number
G0800777
G0800777
260371
Subjects
Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
GRAM-POSITIVE BACTERIA
STAPHYLOCOCCUS-AUREUS
BACILLUS-SUBTILIS
DATA QUALITY
SYNTHASE
BIOSYNTHESIS
MODEL
Bacteria
Cell Wall
Enzyme Catalysis
LTA Synthesis
Lipid
Protein Structure
Amino Acid Sequence
Bacterial Proteins
Catalytic Domain
Crystallography, X-Ray
Escherichia coli
Glycerophosphates
Lipopolysaccharides
Listeria monocytogenes
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Phylogeny
Protein Binding
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins
Static Electricity
Teichoic Acids
06 Biological Sciences
11 Medical And Health Sciences
03 Chemical Sciences
Publication Status
Published