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| <StructureSection load='2hdi' size='340' side='right'caption='[[2hdi]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2hdi' size='340' side='right'caption='[[2hdi]], [[Resolution|resolution]] 2.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2hdi]] is a 2 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=2HDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HDI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hdi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HDI FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</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]] 2.5Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hdf|2hdf]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cirA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), cia ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2hdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hdi OCA], [https://pdbe.org/2hdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hdi RCSB], [https://www.ebi.ac.uk/pdbsum/2hdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hdi 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=2hdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hdi OCA], [https://pdbe.org/2hdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hdi RCSB], [https://www.ebi.ac.uk/pdbsum/2hdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hdi ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/CIRA_ECOLI CIRA_ECOLI]] Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB. [[https://www.uniprot.org/uniprot/CEIA_ECOLX CEIA_ECOLX]] This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy. Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
| + | [https://www.uniprot.org/uniprot/CIRA_ECOLI CIRA_ECOLI] Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB. |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Buchanan, S K]] | + | [[Category: Buchanan SK]] |
- | [[Category: Esser, L]] | + | [[Category: Esser L]] |
- | [[Category: Lukacik, P]] | + | [[Category: Lukacik P]] |
- | [[Category: Antimicrobial protein]]
| + | |
- | [[Category: Colicin i receptor]]
| + | |
- | [[Category: Iron transport]]
| + | |
- | [[Category: Membrane protein]]
| + | |
- | [[Category: Outer membrane]]
| + | |
- | [[Category: Protein transport]]
| + | |
- | [[Category: Receptor ligand]]
| + | |
- | [[Category: Signal transduction]]
| + | |
- | [[Category: Tonb box]]
| + | |
| Structural highlights
Function
CIRA_ECOLI Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB.
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
Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space, where it inserts into the inner membrane and forms a voltage-dependent ion channel. We determined crystal structures of colicin I receptor alone and in complex with the receptor binding domain of colicin Ia. The receptor undergoes large and unusual conformational changes upon colicin binding, opening at the cell surface and positioning the receptor binding domain of colicin Ia directly above it. We modelled the interaction with full-length colicin Ia to show that the channel forming domain is initially positioned 150 A above the cell surface. Functional data using full-length colicin Ia show that colicin I receptor is necessary for cell surface binding, and suggest that the receptor participates in translocation of colicin Ia across the outer membrane.
Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import.,Buchanan SK, Lukacik P, Grizot S, Ghirlando R, Ali MM, Barnard TJ, Jakes KS, Kienker PK, Esser L EMBO J. 2007 May 16;26(10):2594-604. Epub 2007 Apr 26. PMID:17464289[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Buchanan SK, Lukacik P, Grizot S, Ghirlando R, Ali MM, Barnard TJ, Jakes KS, Kienker PK, Esser L. Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import. EMBO J. 2007 May 16;26(10):2594-604. Epub 2007 Apr 26. PMID:17464289
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