Fig. 1 Similar to Figure 2A in the reference paper linked below, we generated a 'map' comparing the proposed LPS phosphate binding sites across species of interest. Each different letter is color-coded to emulate the amino acid view in AliView; each letter corresponds to the standard amino acid nomenclature (e.g. arginine, R; histidine, H; serine, S; etc). Shows the different polymorphisms at crucial binding sites of hemolin and hemolin-like in different species.
This was made by using Su et al Fig 2A to translate H cecropia crystal structure sites to the corresponding M sexta sites. By command-searching the AliView file, relevant site sequences were located (ultimately the correct gene site was 18 ungapped positions greater than the crystal structure sites). Amino acids present at the indicated sites were recorded using the AliView (view AA as 1 position) alignment.
An interesting observation is that a proposed phosphate ion interaction site is 100% conserved among these species. One of the proposed phosphate ion binding sites had the second highest conservation rate (10/11), while the other ion binding site was one of the less conserved sites (7/11).
This was made by using Su et al Fig 2A to translate H cecropia crystal structure sites to the corresponding M sexta sites. By command-searching the AliView file, relevant site sequences were located (ultimately the correct gene site was 18 ungapped positions greater than the crystal structure sites). Amino acids present at the indicated sites were recorded using the AliView (view AA as 1 position) alignment.
An interesting observation is that a proposed phosphate ion interaction site is 100% conserved among these species. One of the proposed phosphate ion binding sites had the second highest conservation rate (10/11), while the other ion binding site was one of the less conserved sites (7/11).