|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3iax' size='340' side='right'caption='[[3iax]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='3iax' size='340' side='right'caption='[[3iax]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3iax]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [https://en.wikipedia.org/wiki/"bacterium_freundii"_braak_1928 "bacterium freundii" braak 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IAX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3iax]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IAX 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0740, JW5100, tolB, UTI89_C0736 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), caa, colA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=546 "Bacterium freundii" Braak 1928])</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=3iax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iax OCA], [https://pdbe.org/3iax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iax RCSB], [https://www.ebi.ac.uk/pdbsum/3iax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iax 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=3iax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iax OCA], [https://pdbe.org/3iax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iax RCSB], [https://www.ebi.ac.uk/pdbsum/3iax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iax ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TOLB_ECOLI TOLB_ECOLI]] Involved in the TonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K). Necessary for the colicins to reach their respective targets after initial binding to the bacteria.[HAMAP-Rule:MF_00671]
| + | [https://www.uniprot.org/uniprot/TOLB_ECOLI TOLB_ECOLI] Involved in the TonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K). Necessary for the colicins to reach their respective targets after initial binding to the bacteria.[HAMAP-Rule:MF_00671] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 37: |
Line 37: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Citrobacter freundii]] |
| - | [[Category: Bacterium freundii braak 1928]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, C]] | + | [[Category: Li C]] |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Antimicrobial]]
| + | |
| - | [[Category: Bacteriocin]]
| + | |
| - | [[Category: Bacteriocin transport]]
| + | |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: Colicin some]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Tolb]]
| + | |
| - | [[Category: Tolb box]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
TOLB_ECOLI Involved in the TonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K). Necessary for the colicins to reach their respective targets after initial binding to the bacteria.[HAMAP-Rule:MF_00671]
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
Interaction of the TolB box of Group A colicins with the TolB protein in the periplasm of Escherichia coli cells promotes transport of the cytotoxic domain of the colicin across the cell envelope. The crystal structure of a complex between a 107-residue peptide (TA(1-107)) of the translocation domain of colicin A (ColA) and TolB identified the TolB box as a 12-residue peptide that folded into a distorted hairpin within a central canyon of the beta-propeller domain of TolB. Comparison of this structure with that of the colicin E9 (ColE9) TolB box-TolB complex, together with site-directed mutagenesis of the ColA TolB box residues, revealed important differences in the interaction of the two TolB boxes with an overlapping binding site on TolB. Substitution of the TolB box residues of ColA with those of ColE9 conferred the ability to competitively recruit TolB from Pal but reduced the biological activity of the mutant ColA. This datum explains (i) the difference in binding affinities of ColA and ColE9 with TolB, and (ii) the inability of ColA, unlike ColE9, to competitively recruit TolB from Pal, allowing an understanding of how these two colicins interact in a different way with a common translocation portal in E. coli cells.
The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins.,Zhang Y, Li C, Vankemmelbeke MN, Bardelang P, Paoli M, Penfold CN, James R Mol Microbiol. 2010 Feb;75(3):623-36. Epub 2009 Jul 21. PMID:19627502[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang Y, Li C, Vankemmelbeke MN, Bardelang P, Paoli M, Penfold CN, James R. The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins. Mol Microbiol. 2010 Feb;75(3):623-36. Epub 2009 Jul 21. PMID:19627502 doi:10.1111/j.1365-2958.2009.06808.x
|
