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1TDP

NMR solution structure of the carnobacteriocin B2 immunity protein

Summary for 1TDP
Entry DOI10.2210/pdb1tdp/pdb
NMR InformationBMRB: 6211
Descriptorcarnobacteriocin B2 immunity protein (1 entity in total)
Functional Keywordsfour-helix bundle, antimicrobial protein
Biological sourceCarnobacterium maltaromaticum
Total number of polymer chains1
Total formula weight12680.63
Authors
Sprules, T.,Kawulka, K.E.,Vederas, J.C. (deposition date: 2004-05-23, release date: 2004-09-28, Last modification date: 2024-05-22)
Primary citationSprules, T.,Kawulka, K.E.,Vederas, J.C.
NMR Solution Structure of ImB2, a Protein Conferring Immunity to Antimicrobial Activity of the Type IIa Bacteriocin, Carnobacteriocin B2
Biochemistry, 43:11740-11749, 2004
Cited by
PubMed 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 solvent. Helix 3 is well-defined to residue 55, and a stretch of nascent helix followed by an unstructured loop joins it to helix 4. No interaction is observed between ImB2 and either carnobacteriocin B2 (CbnB2) or its precursor. Protection from the action of CbnB2 is only observed when ImB2 is expressed within the cell. The loop between helices 3 and 4, and a hydrophobic pocket which it partially masks, may be important for interaction with membrane receptors responsible for sensitivity to class IIa bacteriocins.
PubMed: 15362858
DOI: 10.1021/bi048854+
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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