(A) Ribbon diagrams of PedB (left), EntA-im (middle), and ImB2 (right) shown with secondary structures labeled

<p><b>Copyright information:</b></p><p>Taken from "High resolution crystal structure of PedB: a structural basis for the classification of pediocin-like immunity proteins"</p><p>http://www.biomedcentral.com/1472-6807/7/35</p><p>BMC Structural Biology 2007;7():35-35.</p><p>Published online 30 May 2007</p><p>PMCID:PMC1904221.</p><p></p> The axes of α3 and α4 are indicated by dotted lines. The angle between α3 and α4 is 33° for PedB and 31° for EntA-im. (B) Stereo view of the superimposed structures of PedB (red) and EntA-im (cyan). The flexible C-terminal loop of EntA-im that is thought to be important for its immunity is highlighted by a black ellipse. N and C indicate the N- and C-terminus of PedB, respectively

(A) Sequence alignment of pediocin PP-1 from (pediocinPP) with pediocin PA-1 from (pediocinPA), EnterocinA, and Carnobacteriocin B2 (CarnobacB2)

<p><b>Copyright information:</b></p><p>Taken from "High resolution crystal structure of PedB: a structural basis for the classification of pediocin-like immunity proteins"</p><p>http://www.biomedcentral.com/1472-6807/7/35</p><p>BMC Structural Biology 2007;7():35-35.</p><p>Published online 30 May 2007</p><p>PMCID:PMC1904221.</p><p></p> The substitution between pediocin PP-1 and pediocin PA-1 is indicated by black box. The color scheme of white on dark grey indicates the consensus residue derived from the occurrence of >70% of a single residue at a given position. (B) Structure-based alignment of PedB from (PedB-PP) with PedB from (PedB-PA), EntA-im, and ImB2. Secondary structure of PedB is presented above the alignment. The additional fifth helix of ImB2 is indicated by black bar. The color scheme is same to (A). The conservative substitution between PedB proteins for pediocin PP-1 and pediocin PA-1 is indicated by black box. (C) Pediocin PP-1 susceptibility of strain harboring gene and control plasmid. The MIC is the concentration of bacteriocin that inhibited growth of the indicator strain by 50%. The immunity activity is presented as the -fold increase in MIC observed for strains expressing PedB variants relative to MICs for strains containing only the control plasmid. The results represent the averaged data from at least three experiments. The psodA indicates the promoter of encoding Mn-containing superoxide dismutase in . (D) Determination of oligomeric state of PedB. Oligomeric state of PedB was analysed by gel filtration chromatography. Predicted molecular mass of PedB (See Methods) is 14,428 Da (= 0.42), indicating that PedB exists as a monomer in solution

(A) A graphic display of the immunity activity of strains possessing PedB and PedB variants to pediocin PP-1

<p><b>Copyright information:</b></p><p>Taken from "High resolution crystal structure of PedB: a structural basis for the classification of pediocin-like immunity proteins"</p><p>http://www.biomedcentral.com/1472-6807/7/35</p><p>BMC Structural Biology 2007;7():35-35.</p><p>Published online 30 May 2007</p><p>PMCID:PMC1904221.</p><p></p> The results are presented using the same methods as in Figure 1c. The results represent the averaged data from at least three experiments, and the standard deviation values are indicated in each bar. (B) Far-UV CD spectra of PedB and C-terminal shortened PedB variants. CD spectra (190~250 nm) of 25 μg/ml ml wild type PedB and PedB variants were obtained to compare the secondary structure at 25°C. (C) Near-UV CD spectra of PedB and C-terminal shortened PedB variants. CD spectra (240~360 nm) of 200 μg/ml wild type PedB and PedB variants were obtained to compare the tertiary structure and protein folding at 25°C