Colicin E3: Difference between revisions
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ColE3 initially binds to the BtuB vitamin B12 receptor. Formation of this complex leads to the unfolding of the N terminal receptor binding coiled-coil domain of ColE3<ref> PMID: 17277071 </ref>. | ColE3 initially binds to the BtuB vitamin B12 receptor. Formation of this complex leads to the unfolding of the N terminal receptor binding coiled-coil domain of ColE3<ref> PMID: 17277071 </ref>. | ||
The structure shows the complex formed between BtuB and the ColE3 translocation domain<ref> PMID: 14528295 </ref>. | The structure shows the complex formed between BtuB and the ColE3 translocation domain<ref> PMID: 14528295 </ref>. | ||
Cells with a mutation in the gene encoding the BtuB gene show immunity to ColE3 attack, as well as other [[Colicin]]s that use the same receptor. | |||
After binding to the BtuB receptor, the complex recruits OmpF, and a group of proteins from the [[Tol]] group of proteins, TolQRAB. The mechanism by which these proteins aid the translocation of ColE3 is as yet unknown, but the colicin then traverses the outer membrane and reaches the periplasm. | After binding to the BtuB receptor, the complex recruits OmpF, and a group of proteins from the [[Tol]] group of proteins, TolQRAB. The mechanism by which these proteins aid the translocation of ColE3 is as yet unknown, but the colicin then traverses the outer membrane and reaches the periplasm. | ||