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3fyx
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==The Structure of OmpF porin with a synthetic dibenzo-18-crown-6 as modulator== |
| + | <StructureSection load='3fyx' size='340' side='right' caption='[[3fyx]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3fyx]] is a 1 chain structure with sequence from [http://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=3FYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FYX FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=451:N-(6,7,9,10,17,18,20,21-OCTAHYDRODIBENZO[B,K][1,4,7,10,13,16]HEXAOXACYCLOOCTADECIN-2-YL)ACETAMIDE'>451</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0929, cmlB, coa, cry, JW0912, ompF, tolF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fyx RCSB], [http://www.ebi.ac.uk/pdbsum/3fyx PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fy/3fyx_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The attachment of modulators to a trimeric porin ion channel was investigated (see picture of the trimer with a crown ether modulator (orange)). The interplay of modulator and protein is essential for the conformational heterogeneity of the hybrid channel. Single-site attachment in large pores is not sufficient to change the electrophysiological characteristics of the pores-such change requires additional noncovalent interactions or second-site attachments. | ||
| - | + | On the function and structure of synthetically modified porins.,Reitz S, Cebi M, Reiss P, Studnik G, Linne U, Koert U, Essen LO Angew Chem Int Ed Engl. 2009;48(26):4853-7. PMID:19322865<ref>PMID:19322865</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
==See Also== | ==See Also== | ||
*[[Porin|Porin]] | *[[Porin|Porin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Cebi, M.]] | [[Category: Cebi, M.]] | ||
Revision as of 11:20, 29 September 2014
The Structure of OmpF porin with a synthetic dibenzo-18-crown-6 as modulator
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Categories: Escherichia coli k-12 | Cebi, M. | Essen, L O. | Koert, U. | Reitz, S. | Beta-barrel | Cell membrane | Cell outer membrane | Crown ether | Ion transport | Ion-channel engineering | Membrane | Phage recognition | Porin | Porin structure | Synthetic ion-current modulator | Transmembrane | Transport | Transport protein

