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NMR Solution Structure of ImB2, a Protein Conferring Immunity to Antimicrobial Activity of the Type IIa Bacteriocin, Carnobacteriocin B2

Authors :
Tara Sprules
John C. Vederas
Karen E. Kawulka
Source :
Biochemistry. 43:11740-11749
Publication Year :
2004
Publisher :
American Chemical Society (ACS), 2004.

Abstract

Bacteriocins produced by lactic acid bacteria are potent antimicrobial compounds which are active against closely related bacteria. Producer strains are protected against the effects of their cognate bacteriocins by immunity proteins that are located on the same genetic locus and are coexpressed with the gene encoding the bacteriocin. Several structures are available for class IIa bacteriocins; however, to date, no structures are available for the corresponding immunity proteins. We report here the NMR solution structure of the 111-amino acid immunity protein for carnobacteriocin B2 (ImB2). ImB2 folds into a globular domain in aqueous solution which contains an antiparallel four-helix bundle. Extensive packing by hydrophobic side chains in adjacent helices forms the core of the protein. The C-terminus, containing a fifth helix and an extended strand, is held against the four-helix bundle by hydrophobic interactions with helices 3 and 4. Most of the charged and polar residues in the protein face the solven...

Details

ISSN :
15204995 and 00062960
Volume :
43
Database :
OpenAIRE
Journal :
Biochemistry
Accession number :
edsair.doi...........94def5c19995b6058c5d43e12d16240e