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Figure 2 | BMC Structural Biology

Figure 2

From: Crystal structure of c5321: a protective antigen present in uropathogenic Escherichia coli strains displaying an SLR fold

Figure 2

Sequences of the eleven SLR repeats of c5321, aligned with the SLR consensus sequence. First two rows provide a counter for intra-SLR position (first digit of the counter given in first row and second digit in second row). Second column corresponds to sequence number in full-length protein of first residue in the row. Specific amino-acid residues in the consensus sequence (from the SMART database [5]) are indicated with capital letters, while lower case letters stand for: p-polar; h-hydrophobic; t-turn like; s-small; c-charged; a-aromatic; l-leucine, valine or isoleucine. Secondary-structure elements are outlined in the last row, with loop regions being represented by hyphens (except SLR9, where helix2 is longer at the expense of the standard intra-repeat loop length). Residues matching specific conserved amino acids in the SLR consensus sequence are coloured in orange, while consensus amino-acid types with a dominant representative in c5321 SLR units are shown in blue (with the exception of W28r, which is coloured green for easy identification).

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