2j1n: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2j1n.png|left|200px]]
-<!--
+==osmoporin OmpC==
-The line below this paragraph, containing "STRUCTURE_2j1n", creates the "Structure Box" on the page.
+<StructureSection load='2j1n' size='340' side='right'caption='[[2j1n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2j1n]] is a 3 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=2J1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J1N FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_2j1n|  PDB=2j1n  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j1n OCA], [https://pdbe.org/2j1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j1n RCSB], [https://www.ebi.ac.uk/pdbsum/2j1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j1n ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/OMPC_ECOLI OMPC_ECOLI] Forms pores that allow passive diffusion of small molecules across the outer membrane.
+== 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/j1/2j1n_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/main_output.php?pdb_ID=2j1n ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Porins form transmembrane pores in the outer membrane of Gram-negative bacteria with matrix porin OmpF and osmoporin OmpC from Escherichia coli being differentially expressed depending on environmental conditions. The three-dimensional structure of OmpC has been determined to 2.0 A resolution by X-ray crystallography. As expected from the high sequence similarity, OmpC adopts the OmpF-like 16-stranded hollow beta-barrel fold with three beta-barrels associated to form a tight trimer. Unlike in OmpF, the extracellular loops form a continuous wall at the perimeter of the vestibule common to the three pores, due to a 14-residues insertion in loop L4. The pore constriction and the periplasmic outlet are very similar to OmpF with 74% of the pore lining residues being conserved. Overall, only few ionizable residues are exchanged at the pore lining. The OmpC structure suggests that not pore size, but electrostatic pore potential and particular atomic details of the pore linings are the critical parameters that physiologically distinguish OmpC from OmpF.
-===OSMOPORIN OMPC===
+Crystal structure of osmoporin OmpC from E. coli at 2.0 A.,Basle A, Rummel G, Storici P, Rosenbusch JP, Schirmer T J Mol Biol. 2006 Oct 6;362(5):933-42. Epub 2006 Aug 3. PMID:16949612<ref>PMID:16949612</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16949612}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2j1n" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16949612 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_16949612}}
-==About this Structure==
-[[2j1n]] is a 3 chain structure of [[Porin]] with 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=2J1N OCA].
 ==See Also==
 *[[Porin|Porin]]
+*[[Porin 3D structures|Porin 3D structures]]
-==Reference==
+== References ==
-<ref group="xtra">PMID:016949612</ref><references group="xtra"/>
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Basle, A.]]
+[[Category: Large Structures]]
-[[Category: Rosenbusch, J P.]]
+[[Category: Basle A]]
-[[Category: Rummel, G.]]
+[[Category: Rosenbusch JP]]
-[[Category: Schirmer, T.]]
+[[Category: Rummel G]]
-[[Category: Storici, P.]]
+[[Category: Schirmer T]]
-[[Category: Beta-barrel]]
+[[Category: Storici P]]
-[[Category: Ion transport]]
-[[Category: Osmoporin]]
-[[Category: Transport protein]]