TolB: Difference between revisions
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{{STRUCTURE_1c5k| PDB=1c5k | SIZE=400| SCENE=TolB/Tolb/1 |right|CAPTION=E. coli TolB, [[1c5k]] }} | {{STRUCTURE_1c5k| PDB=1c5k | SIZE=400| SCENE=TolB/Tolb/1 |right|CAPTION=E. coli TolB, [[1c5k]] }} | ||
==Structure== | ==Structure== | ||
TolB is a 44-kDa periplasmic protein partially associated with the outer membrane<ref name='Bouveret'>PMID: 7744736</ref>. It has two domains: an N-terminal α/β domain and a C-terminal six-bladed β-propeller (to which [[Pal]] and [[Colicin E9]] bind)<ref name='Bonsor'>PMID: 19696740</ref>. The β-propeller has a latching or ‘Velco’ strand which joins the first and last of the six blades, and is positioned in the domain-domain interface. When Pal binds to the C-terminus of TolB, the latching strand moves away from the interface and carries with it a proline residue. The movement of the latching strand opens up a canyon that would normally be buried between the N- and C-terminal domains of TolB. This canyon can now be used as a binding site for the N-terminal of TolB, which forms a helical half-turn and a β-sheet against the canyon. | TolB is a 44-kDa periplasmic protein partially associated with the outer membrane<ref name='Bouveret'>PMID: 7744736</ref>. It has two domains: an N-terminal α/β domain and a C-terminal six-bladed β-propeller (to which [[Pal]] and [[Colicin E9]] bind)<ref name='Bonsor'>PMID: 19696740</ref>. The β-propeller has a latching or ‘Velco’ strand which joins the first and last of the six blades, and is positioned in the domain-domain interface. When Pal binds to the C-terminus of TolB, the latching strand moves away from the interface and carries with it a proline residue. The movement of the latching strand opens up a canyon that would normally be buried between the N- and C-terminal domains of TolB. This canyon can now be used as a binding site for the N-terminal of TolB, which forms a helical half-turn and a β-sheet against the canyon. | ||
