Abstract
In bacteria, the synthesis of the protective peptidoglycan sacculus is a dynamic process that is tightly regulated at multiple levels. Recently, the lipoprotein co-factor LpoB has been found essential for the in vivo function of the major peptidoglycan synthase PBP1b in Enterobacteriaceae. Here, we reveal the crystal structures of Salmonella enterica and Escherichia coli LpoB. The LpoB protein can be modeled as a ball and tether, consisting of a disordered N-terminal region followed by a compact globular C-terminal domain. Taken together, our structural data allow us to propose new insights into LpoB-mediated regulation of peptidoglycan synthesis.
Keywords:
Bacteria; Cell Wall; Lipoprotein; Penicillin-binding Protein; Peptidoglycan; Regulation; X-ray Crystallography.
© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Outer Membrane Proteins / chemistry*
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Bacterial Outer Membrane Proteins / metabolism*
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Cell Membrane / metabolism*
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Crystallography, X-Ray
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Escherichia coli / cytology
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Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / metabolism*
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Lipoproteins / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Penicillin-Binding Proteins / metabolism*
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Peptidoglycan Glycosyltransferase / metabolism*
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Protein Multimerization
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Protein Structure, Quaternary
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Protein Structure, Secondary
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Salmonella enterica / cytology
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Salmonella enterica / metabolism*
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Serine-Type D-Ala-D-Ala Carboxypeptidase / metabolism*
Substances
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Bacterial Outer Membrane Proteins
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Escherichia coli Proteins
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Lipoproteins
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LpoB protein, E coli
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Penicillin-Binding Proteins
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Peptidoglycan Glycosyltransferase
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penicillin-binding protein 1B, E coli
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Serine-Type D-Ala-D-Ala Carboxypeptidase