Anthrax Lethal Factor: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Peter Aziz (talk | contribs) No edit summary |
Peter Aziz (talk | contribs) No edit summary |
||
| Line 43: | Line 43: | ||
Anthrax Lethal Factor is composed of four domains: | Anthrax Lethal Factor is composed of four domains: | ||
'''Domain I''' functions in the binding of Lethal Factor to Protective Antigen 63 (PA63), which is the membrane translocation component of Anthrax Toxin.<ref name=Collier>PMID: 14570563</ref> The actual location where <scene name='Anthrax_Lethal_Factor/Domain_1/1'>domain I</scene> interacts with PA is unknown. This domain, made up of amino acids residues 1-263, is perched above the other three domains and is connected to the rest of the domains through an abrupt turn at the end of the last helix.<ref name=Collier>PMID: 14570563</ref> Domain I consist of 12-helix bundle, packs against one face of a mixed four-stranded beta-sheet.<ref name=Collier>PMID: 14570563</ref> <ref name=Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C, Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P, Liddington RC>PMID: 11700563</ref> | '''<scene name='Anthrax_Lethal_Factor/Domain_-1-/1'>Domain I</scene>''' functions in the binding of Lethal Factor to Protective Antigen 63 (PA63), which is the membrane translocation component of Anthrax Toxin.<ref name=Collier>PMID: 14570563</ref> The actual location where <scene name='Anthrax_Lethal_Factor/Domain_1/1'>domain I</scene> interacts with PA is unknown. This domain, made up of amino acids residues 1-263, is perched above the other three domains and is connected to the rest of the domains through an abrupt turn at the end of the last helix.<ref name=Collier>PMID: 14570563</ref> Domain I consist of 12-helix bundle, packs against one face of a mixed four-stranded beta-sheet.<ref name=Collier>PMID: 14570563</ref> <ref name=Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C, Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P, Liddington RC>PMID: 11700563</ref> | ||
'''Domain II''' consist of residues 263-297 and 385-550; also it has a similar structure with that of B. Cereus toxin catalytic domain VIP2, which contains a NAD binding pocket. Lethal Factor domain II lacks ADP-ribosylating activity due to the lack of conserved residues.<ref name=Collier>PMID: 14570563</ref> <ref name=Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C, Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P, Liddington RC>PMID: 11700563</ref> | '''Domain II''' consist of residues 263-297 and 385-550; also it has a similar structure with that of B. Cereus toxin catalytic domain VIP2, which contains a NAD binding pocket. Lethal Factor domain II lacks ADP-ribosylating activity due to the lack of conserved residues.<ref name=Collier>PMID: 14570563</ref> <ref name=Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C, Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P, Liddington RC>PMID: 11700563</ref> | ||
