Residues of Heat - Labile Enterotoxin Involved in 7 Bacterial Cell
نویسندگان
چکیده
9 Running title: Surface binding mutants of LT 10 11 12 Benjamin Mudrak 1 , Daniel L. Rodriguez 2 , and Meta J. Kuehn 1,2* 13 Departments of Molecular Genetics and Microbiology 1 and Biochemistry 2 14 Duke University Medical Center, Durham, NC 27710 15 16 17 18 19 20 21 * To whom correspondence should be addressed: Tel. 919-684-2545; Fax 919-684-8885; 22 E-mail: [email protected] 23 Copyright © 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved. J. Bacteriol. doi:10.1128/JB.01622-08 JB Accepts, published online ahead of print on 6 March 2009
منابع مشابه
Effect of site-directed mutagenic alterations on ADP-ribosyltransferase activity of the A subunit of Escherichia coli heat-labile enterotoxin.
Previous studies of the S1 subunit of pertussis toxin, an NAD(+)-dependent ADP-ribosyltransferase, suggested that a small amino-terminal region of amino acid sequence similarity to the active fragments of both cholera toxin and Escherichia coli heat-labile enterotoxin represents a region containing critical active-site residues that might be involved in the binding of the substrate NAD+. Other ...
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