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Figure 1 | BMC Structural Biology

Figure 1

From: High resolution crystal structure of PedB: a structural basis for the classification of pediocin-like immunity proteins

Figure 1

(A) Sequence alignment of pediocin PP-1 from P. pentosaceus (pediocinPP) with pediocin PA-1 from P. acidilactici (pediocinPA), EnterocinA, and Carnobacteriocin B2 (CarnobacB2). 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 P. pentosaceus (PedB-PP) with PedB from P. acidilactici (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 L. sakei strain harboring pedB 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 sodA encoding Mn-containing superoxide dismutase in B. subtilis. (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 (Kav = 0.42), indicating that PedB exists as a monomer in solution.

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