2f1t

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[[Image:2f1t.gif|left|200px]]
 
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{{Structure
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==Outer membrane protein OmpW==
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|PDB= 2f1t |SIZE=350|CAPTION= <scene name='initialview01'>2f1t</scene>, resolution 3.0&Aring;
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<StructureSection load='2f1t' size='340' side='right'caption='[[2f1t]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>
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<table><tr><td colspan='2'>[[2f1t]] is a 3 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=2F1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F1T FirstGlance]. <br>
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|ACTIVITY=
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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&#8491;</td></tr>
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|GENE= ompW ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr>
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|DOMAIN=
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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=2f1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1t OCA], [https://pdbe.org/2f1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f1t RCSB], [https://www.ebi.ac.uk/pdbsum/2f1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f1t ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1t OCA], [http://www.ebi.ac.uk/pdbsum/2f1t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f1t RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/OMPW_ECOLI OMPW_ECOLI] Acts as a receptor for colicin S4.<ref>PMID:10348872</ref>
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== Evolutionary Conservation ==
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'''Outer membrane protein OmpW'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f1/2f1t_consurf.spt"</scriptWhenChecked>
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Escherichia coli OmpW belongs to a family of small outer membrane proteins that are widespread in Gram-negative bacteria. Their functions are unknown, but recent data suggest that they may be involved in the protection of bacteria against various forms of environmental stress. To gain insight into the function of these proteins A we have determined the crystal structure of E. coli OmpW to 2.7-A resolution. The structure shows that OmpW forms an 8-stranded beta-barrel with a long and narrow hydrophobic channel that contains a bound n-dodecyl-N,N-dimethylamine-N-oxide detergent molecule. Single channel conductance experiments show that OmpW functions as an ion channel in planar lipid bilayers. The channel activity can be blocked by the addition of n-dodecyl-N,N-dimethylamine-N-oxide. Taken together, the data suggest that members of the OmpW family could be involved in the transport of small hydrophobic molecules across the bacterial outer membrane.
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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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==About this Structure==
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</jmolCheckbox>
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2F1T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1T OCA].
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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=2f1t ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel., Hong H, Patel DR, Tamm LK, van den Berg B, J Biol Chem. 2006 Mar 17;281(11):7568-77. Epub 2006 Jan 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16414958 16414958]
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<references/>
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[[Category: Escherichia coli]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Berg, B van den.]]
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[[Category: Escherichia coli K-12]]
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[[Category: beta barrel]]
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[[Category: Large Structures]]
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[[Category: outer membrane protein]]
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[[Category: Van den Berg B]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:56:43 2008''
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Current revision

Outer membrane protein OmpW

PDB ID 2f1t

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