Sandbox Reserved 1600: Difference between revisions

[[Image:Aligmentbdoidase.jpg|200 px|left|thumb|Figure 5. Alignment of bd oxidase for the organisms ''G. thermodenitrificans'' (PDB: [[5doq]]) shown in <font color='blue'><b>blue</b></font> and ''E. coli'' (PDB: [[6rko]]) shown in <font color='purple'><b>purple</b></font>.]] [[Image:Heme alignment.png|200 px|right|thumb|Figure 6. Heme arrangements for the organisms ''G. thermodenitrificans'' and ''E. coli''. Heme D (green); Heme B595 and Heme B558 shown in pink]] The structure of bd oxidase for ''G. thermodenitrificans'' is highly similar to the structure of [[6rko| bd oxidase in ''E. coli'']] with the major differentiation being the length of the Q-loop.<ref name= ”Theßeling”>PMID:31723136</ref> The similarities and differences between the two proteins can be seen in the alignment of their main structures (Fig.5). Although only having one significant difference in structure, this shift in the X-loop causes the two proteins to have different active sites (Fig. 6). In particular, the <scene name='83/838655/Hemes_ecoli/2'> hemes of bd oxidase in E. coli </scene> are arranged differently than the <scene name='83/838655/Hemes/4'>hemes of bd oxidase in ''G. thermodenitrificans''</scene>. The main reason for this change in heme arrangement is because of the <scene name='83/838655/Oxygen_site_ecoli/1'>oxygen binding site</scene> being located differently in [https://en.wikipedia.org/wiki/Escherichia_coli ''E. coli''], thus causing a different active site arrangement in the protein.<ref name = ”Theßeling” />