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| | <StructureSection load='1rh1' size='340' side='right'caption='[[1rh1]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1rh1' size='340' side='right'caption='[[1rh1]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rh1]] is a 1 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=1RH1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RH1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rh1]] is a 1 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=1RH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RH1 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh1 OCA], [http://pdbe.org/1rh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rh1 RCSB], [http://www.ebi.ac.uk/pdbsum/1rh1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh1 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=1rh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh1 OCA], [https://pdbe.org/1rh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rh1 RCSB], [https://www.ebi.ac.uk/pdbsum/1rh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/CEAB_ECOLX CEAB_ECOLX] |
| - | Colicin B (55 kDa) is a cytotoxic protein that recognizes the outer membrane transporter, FepA, as a receptor and, after gaining access to the cytoplasmic membranes of sensitive Escherichia coli cells, forms a pore that depletes the electrochemical potential of the membrane and ultimately results in cell death. To begin to understand the series of dynamic conformational changes that must occur as colicin B translocates from outer membrane to cytoplasmic membrane, we report here the crystal structure of colicin B at 2.5 A resolution. The crystal belongs to the space group C2221 with unit cell dimensions a = 132.162 A, b = 138.167 A, c = 106.16 A. The overall structure of colicin B is dumbbell shaped. Unlike colicin Ia, the only other TonB-dependent colicin crystallized to date, colicin B does not have clearly structurally delineated receptor-binding and translocation domains. Instead, the unique N-terminal lobe of the dumbbell contains both domains and consists of a large (290 residues), mostly beta-stranded structure with two short alpha-helices. This is followed by a single long ( approximately 74 A) helix that connects the N-terminal domain to the C-terminal pore-forming domain, which is composed of 10 alpha-helices arranged in a bundle-type structure, similar to the pore-forming domains of other colicins. The TonB box sequence at the N-terminus folds back to interact with the N-terminal lobe of the dumbbell and leaves the flanking sequences highly disordered. Comparison of sequences among many colicins has allowed the identification of a putative receptor-binding domain.
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| - | Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution.,Hilsenbeck JL, Park H, Chen G, Youn B, Postle K, Kang C Mol Microbiol. 2004 Feb;51(3):711-20. PMID:14731273<ref>PMID:14731273</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 1rh1" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Colicin 3D structures|Colicin 3D structures]] | | *[[Colicin 3D structures|Colicin 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, G]] | + | [[Category: Chen G]] |
| - | [[Category: Hilsenbeck, J L]] | + | [[Category: Hilsenbeck JL]] |
| - | [[Category: Kang, C]] | + | [[Category: Kang C]] |
| - | [[Category: Park, H]] | + | [[Category: Park H]] |
| - | [[Category: Postle, K]] | + | [[Category: Postle K]] |
| - | [[Category: Youn, B]] | + | [[Category: Youn B]] |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Colicin b]]
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| - | [[Category: Cytotoxic bacterial protein]]
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| - | [[Category: Fepa]]
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| - | [[Category: Tonb]]
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