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. 2014 Sep;196(18):3279–3288. doi: 10.1128/JB.01910-14

FIG 1.

FIG 1

X-ray crystal structure of P. mirabilis Crl. (A) Ribbon model of P. mirabilis Crl with a color gradient of blue to red from the N to the C terminus. Secondary-structure elements are labeled. (B) Amino acid sequence alignment of Crl homologs from P. mirabilis (YP_002150140.1), E. coli (NP_414775.1), S. enterica (NP_454931.1), Aeromonas hydrophila (YP_857911.1), V. harveyi (YP_001444378.1), Photobacterium profundum (YP_129053.1), and Psychromonas ingrahamii (YP_944255.1). Structural elements are indicated above the sequences, and 100% conserved sequences are indicated by red shading. Residues in red letters are similar within a group. Residues framed in blue are similar across groups. The relative surface accessibility (acc) of each residue is plotted below the sequences as a colored box: dark blue for accessible, cyan for intermediate, and white for buried. Red indicates no prediction. (C) Evolutionarily conserved amino acids on a surface view of P. mirabilis Crl. Conservation was determined using ConSurf and is displayed in greyscale with light to dark colors indicating more to less conserved; 100% conserved residues are shown in red. (D) Predicted electrostatic surface of P. mirabilis Crl generated using Pymol.