Document Detail

Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site.
MedLine Citation:
PMID:  23796240     Owner:  NLM     Status:  MEDLINE    
Proteins with LytM (Peptidase_M23) domains are broadly distributed in bacteria and have been implicated in a variety of important processes, including cell division and cell-shape determination. Most LytM-like proteins that have been structurally and/or biochemically characterized are metallo-endopeptidases that cleave cross-links in the peptidoglycan (PG) cell wall matrix. Notable exceptions are the Escherichia coli cell division proteins EnvC and NlpD. These LytM factors are not hydrolases themselves, but instead serve as activators that stimulate PG cleavage by target enzymes called amidases to promote cell separation. Here we report the structure of the LytM domain from EnvC, the first structure of a LytM factor implicated in the regulation of PG hydrolysis. As expected, the fold is highly similar to that of other LytM proteins. However, consistent with its role as a regulator, the active-site region is degenerate and lacks a catalytic metal ion. Importantly, genetic analysis indicates that residues in and around this degenerate active site are critical for amidase activation in vivo and in vitro. Thus, in the regulatory LytM factors, the apparent substrate binding pocket conserved in active metallo-endopeptidases has been adapted to control PG hydrolysis by another set of enzymes.
Nick T Peters; Cécile Morlot; Desirée C Yang; Tsuyoshi Uehara; Thierry Vernet; Thomas G Bernhardt
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2013-07-23
Journal Detail:
Title:  Molecular microbiology     Volume:  89     ISSN:  1365-2958     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2013 Aug 
Date Detail:
Created Date:  2013-08-12     Completed Date:  2014-03-10     Revised Date:  2014-08-04    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  690-701     Citation Subset:  IM    
Copyright Information:
© 2013 John Wiley & Sons Ltd.
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MeSH Terms
Amidohydrolases / metabolism
Amino Acid Sequence
Catalytic Domain
Crystallography, X-Ray
DNA Mutational Analysis
Endopeptidases / chemistry*,  genetics,  metabolism*
Escherichia coli / enzymology*
Escherichia coli Proteins / chemistry*,  genetics,  metabolism*
Models, Molecular
Molecular Sequence Data
Protein Conformation
Sequence Alignment
Grant Support
Reg. No./Substance:
0/Escherichia coli Proteins; EC 3.4.-/Endopeptidases; EC 3.4.-/YibP protein, E coli; EC 3.5.-/Amidohydrolases

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