1a87

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(New page: 200px<br /><applet load="1a87" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a87, resolution 3.1&Aring;" /> '''COLICIN N'''<br /> =...)
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[[Image:1a87.gif|left|200px]]<br /><applet load="1a87" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1a87, resolution 3.1&Aring;" />
 
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'''COLICIN N'''<br />
 
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==Overview==
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==COLICIN N==
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BACKGROUND: Pore-forming colicins are water-soluble bacteriocins capable, of binding to and translocating through the Escherichia coli cell, envelope. They then undergo a transition to a transmembrane ion channel in, the cytoplasmic membrane leading to bacterial death. Colicin N is the, smallest pore-forming colicin known to date (40 kDa instead of the more, usual 60 kDa) and the crystal structure of its membrane receptor, the, porin OmpF, is already known. Structural knowledge of colicin N is, therefore important for a molecular understanding of colicin toxicity and, is relevant to toxic mechanisms in general. RESULTS: The crystal structure, of colicin N reveals a novel receptor-binding domain containing a, six-stranded antiparallel beta sheet wrapped around the 63 A long, N-terminal alpha helix of the pore-forming domain. The pore-forming domain, adopts a ten alpha-helix bundle that has been observed previously in the, pore-forming domains of colicin A, la and E1. The translocation domain, however, does not appear to adopt any regular structure. Models for, receptor binding and translocation through the outer membrane are proposed, based on the structure and biochemical data. CONCLUSIONS: The colicin, N-ompF system is now the structurally best-defined translocation pathway., Knowledge of the colicin N structure, coupled with the structure of its, receptor, OmpF, and previously published biochemical data, limits the, numerous possibilities of translocation and leads to a model in which the, translocation domain inserts itself through the porin pore, the, receptor-binding domain stays outside and the pore-forming domain, translocates along the outer wall of the trimeric porin channel.
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<StructureSection load='1a87' size='340' side='right'caption='[[1a87]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1a87]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A87 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a87 OCA], [https://pdbe.org/1a87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a87 RCSB], [https://www.ebi.ac.uk/pdbsum/1a87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a87 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CEAN_ECOLX CEAN_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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a87_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a87 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1A87 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A87 OCA].
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*[[Colicin 3D structures|Colicin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of a colicin N fragment suggests a model for toxicity., Vetter IR, Parker MW, Tucker AD, Lakey JH, Pattus F, Tsernoglou D, Structure. 1998 Jul 15;6(7):863-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9687368 9687368]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Lakey JH]]
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[[Category: Lakey, J.H.]]
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[[Category: Parker MW]]
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[[Category: Parker, M.W.]]
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[[Category: Pattus F]]
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[[Category: Pattus, F.]]
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[[Category: Tsernoglou D]]
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[[Category: Tsernoglou, D.]]
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[[Category: Tucker AD]]
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[[Category: Tucker, A.D.]]
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[[Category: Vetter IR]]
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[[Category: Vetter, I.R.]]
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[[Category: bacteriocin]]
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[[Category: pore-forming activity]]
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[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:40:34 2007''
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Current revision

COLICIN N

PDB ID 1a87

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