The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure

Journal of Bacteriology

Volumn 178, Issue 18, 1996, Pages 5402-5409

  Goffin, Colette ^a   Fraipont, Claudine ^a   Ayala, Juan ^b   Terrak, Mohammed ^a   Nguyen Distèche, Martine ^a   Ghuysen, Jean Marie ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CHAPERONE; PENICILLIN BINDING PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CELL DIVISION; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE;

ESCHERICHIA COLI; STREPTOCOCCUS PNEUMONIAE;

EID: 0029808359     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.18.5402-5409.1996     Document Type: Article

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