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2ivz

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Revision as of 10:33, 12 January 2022

Structure of TolB in complex with a peptide of the colicin E9 T- domain

Structural highlights

2ivz is a 8 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1bxi, 1c5k, 1crz, 1emv, 1fr2, 1fsj, 1v13, 1v14, 1v15
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CEA9_ECOLX] This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity. Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The natively disordered N-terminal 83-aa translocation (T) domain of E group nuclease colicins recruits OmpF to a colicin-receptor complex in the outer membrane (OM) as well as TolB in the periplasm of Escherichia coli, the latter triggering translocation of the toxin across the OM. We have identified the 16-residue TolB binding epitope in the natively disordered T-domain of the nuclease colicin E9 (ColE9) and solved the crystal structure of the complex. ColE9 folds into a distorted hairpin within a canyon of the six-bladed beta-propeller of TolB, using two tryptophans to bolt the toxin to the canyon floor and numerous intramolecular hydrogen bonds to stabilize the bound conformation. This mode of binding enables colicin side chains to hydrogen-bond TolB residues in and around the channel that runs through the beta-propeller and that constitutes the binding site of peptidoglycan-associated lipoprotein (Pal). Pal is a globular binding partner of TolB, and their association is known to be important for OM integrity. The structure is therefore consistent with translocation models wherein the colicin disrupts the TolB-Pal complex causing local instability of the OM as a prelude to toxin import. Intriguingly, Ca(2+) ions, which bind within the beta-propeller channel and switch the surface electrostatics from negative to positive, are needed for the negatively charged T-domain to bind TolB with an affinity equivalent to that of Pal and competitively displace it. Our study demonstrates that natively disordered proteins can compete with globular proteins for binding to folded scaffolds but that this can require cofactors such as metal ions to offset unfavorable interactions.

Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9.,Loftus SR, Walker D, Mate MJ, Bonsor DA, James R, Moore GR, Kleanthous C Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12353-8. Epub 2006 Aug 7. PMID:16894158^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Loftus SR, Walker D, Mate MJ, Bonsor DA, James R, Moore GR, Kleanthous C. Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12353-8. Epub 2006 Aug 7. PMID:16894158

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ivz"

@@ Line 3: / Line 3: @@
 <StructureSection load='2ivz' size='340' side='right'caption='[[2ivz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ivz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IVZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IVZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ivz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IVZ FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bxi|1bxi]], [[1c5k|1c5k]], [[1crz|1crz]], [[1emv|1emv]], [[1fr2|1fr2]], [[1fsj|1fsj]], [[1v13|1v13]], [[1v14|1v14]], [[1v15|1v15]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bxi|1bxi]], [[1c5k|1c5k]], [[1crz|1crz]], [[1emv|1emv]], [[1fr2|1fr2]], [[1fsj|1fsj]], [[1v13|1v13]], [[1v14|1v14]], [[1v15|1v15]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2ivz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ivz OCA], [http://pdbe.org/2ivz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ivz RCSB], [http://www.ebi.ac.uk/pdbsum/2ivz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ivz ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ivz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ivz OCA], [https://pdbe.org/2ivz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ivz RCSB], [https://www.ebi.ac.uk/pdbsum/2ivz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ivz ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CEA9_ECOLX CEA9_ECOLX]] This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity.  Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
+[[https://www.uniprot.org/uniprot/CEA9_ECOLX CEA9_ECOLX]] This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity.  Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
 *[[Colicin 3D structures|Colicin 3D structures]]
-*[[Tol|Tol]]
 *[[TolB|TolB]]
 *[[TonB|TonB]]

2ivz

From Proteopedia

Revision as of 10:33, 12 January 2022

Structure of TolB in complex with a peptide of the colicin E9 T- domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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