TolB: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Laura McCauley, Michal Harel, Joel L. Sussman

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-{{STRUCTURE_1c5k|  PDB=1c5k  | SIZE=400| SCENE=TolB/Tolb/1 |right|CAPTION=E. coli TolB, [[1c5k]] }}
+<StructureSection load='' size='350' side='right' scene='TolB/Tolb/1' caption='E. coli TolB (PDB code [[1c5k]])'>
 ==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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 ==The TolB-Pal Complex==
-<structure load='2w8b' size='300' align='left' caption='Interaction of TolB and peptoglycan-associated lipoprotein (Pal) [[2w8b]]' (PDB entry [[2w8b]]  |  SCENE= TolB/Tolbpal/1 />The TolB-[[Pal]] complex is involved in maintaining the outer membrane integrity.  Upon binding, TolB and Pal undergo a conformational change , the result of which is crucial for further interactions with other proteins<ref name='Godlewska'>PMID: 19519769</ref>.  This complex is parasitised by protein antibiotics  and disrupted in order to trigger the translocation of the toxin across the outer membrane (see [[Colicin]] for further information)<ref name='Bonsor'>PMID: 17375930</ref>.
-To study the interaction of TolB with Pal, two studies were carried out<ref name='Bouveret'>PMID 7744736</ref>: TolBBep (tagging TolB for immunoprecipitation), which allows the associated proteins to remain in contact with TolB, and ''in vivo'' cross-linking experiments with formaldehyde.  Immunoprecipitation gave the result that Pal co-precipitates with TolBBep, while the cross-linking showed that in the present of Pal, the two products migrated close to each other, but in the absence of Pal, neither band was present, demonstrating an interaction between the two.  These two experiments showed that TolB directly interacts with Pal, and that this interaction is responsible for maintaining the association of TolB with the membrane.
+The TolB-[[Pal]] complex is involved in maintaining the outer membrane integrity.  Upon binding, TolB and Pal undergo a conformational change , the result of which is crucial for further interactions with other proteins<ref name='Godlewska'>PMID: 19519769</ref>.  This complex is parasitised by protein antibiotics  and disrupted in order to trigger the translocation of the toxin across the outer membrane (see [[Colicin]] for further information)<ref name='Bonsor'>PMID: 17375930</ref>.
+To study the interaction of TolB with Pal, two studies were carried out<ref name='Bouveret'>PMID 7744736</ref>: TolBBep (tagging TolB for immunoprecipitation), which allows the associated proteins to remain in contact with TolB, and ''in vivo'' cross-linking experiments with formaldehyde.  Immunoprecipitation gave the result that Pal co-precipitates with TolBBep, while the cross-linking showed that in the present of Pal, the two products migrated close to each other, but in the absence of Pal, neither band was present, demonstrating an interaction between the two.  These two experiments showed that TolB directly interacts with Pal, and that this interaction is responsible for maintaining the association of TolB with the membrane.
+{{STRUCTURE_2hqs|  PDB=2hqs  | SIZE=300| SCENE= |left|CAPTION=E. coli TolB (cyan) complex with peptidoglycan-associated lipoprotein (gold), acetate, sulfate and glycerol, (PDB code = [[2hgs]]) }}
+</StructureSection>
 ==3D structures of TolB==
-[[1crg]], [[1c5k]] – EcTolB – ''Escherichia coli''<br />
+Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+[[1crz]], [[1c5k]] – EcTolB – ''Escherichia coli''<br />
 [[2ivz]] – EcTolB + colicin-E9 T-domain<br />
+[[4jml]] - EcTolB (mutant) + colicin-E9 T-domain (mutant)<br />
+[[7nst]] - EcTolB (mutant) + colicin-E9 + outer membrane protein F – Cryo EM<br />
+[[7nsu]] - EcTolB (mutant) + colicin-E9 + outer membrane protein F + BtuB – Cryo EM<br />
 [[3iax]] - EcTolB + colicin-A translocation domain<br />
-[[2hqs]], [[2w8b]] - EcTolB + peptidoglycan-associated lipoprotein
+[[2hqs]], [[2w8b]] - EcTolB + peptidoglycan-associated lipoprotein<br />
+[[4pwz]] – YpTolB – ''Yersinia pestis''<br />
+[[4r40]] - YpTolB + peptidoglycan-associated lipoprotein<br />
+[[6pnv]] – TolB – ''Salmonella enterica''<br />
+[[7mx5]] – TolB – ''Acinetobacteria baumannii''<br />
 == References==
 <references/>
+[[Category: Topic Page]]