TolB: Difference between revisions

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==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. For additional details see [[Tol]].

==Function==

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 ==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.  For additional details see [[Tol]].
 ==Function==