Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site

Molecular Microbiology

Volumn 89, Issue 4, 2013, Pages 690-701

  Peters, Nick T ^a   Morlot, Cécile ^b,c,d   Yang, Desirée C ^a   Uehara, Tsuyoshi ^a   Vernet, Thierry ^b,c,d   Bernhardt, Thomas G ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b CEA GRENOBLE   (France)

^c CNRS   (France)

^d UNIV GRENOBLE ALPES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; BACTERIAL PROTEIN; ENVC PROTEIN; LYTM PROTEIN; METAL ION; METALLOPROTEINASE; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CELL DIVISION; CELL WALL; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; ESCHERICHIA COLI; GENETIC ANALYSIS; HYDROLYSIS; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; REGULATORY MECHANISM; STRUCTURE ACTIVITY RELATION;

ESCHERICHIA COLI;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DNA MUTATIONAL ANALYSIS; ENDOPEPTIDASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

EID: 84881550004     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12304     Document Type: Article

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