2eyb: Difference between revisions

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-{{Seed}}
-[[Image:2eyb.png|left|200px]]
-<!--
+==Water refined solution structure of crambin in ACETONE/WATER==
-The line below this paragraph, containing "STRUCTURE_2eyb", creates the "Structure Box" on the page.
+<StructureSection load='2eyb' size='340' side='right'caption='[[2eyb]]' 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'>[[2eyb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EYB 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">Solution NMR, 20 models</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=2eyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eyb OCA], [https://pdbe.org/2eyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eyb RCSB], [https://www.ebi.ac.uk/pdbsum/2eyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eyb ProSAT]</span></td></tr>
-{{STRUCTURE_2eyb|  PDB=2eyb  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known.
+== 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/ey/2eyb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2eyb ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We chose crambin, a hydrophobic and water-insoluble protein originally isolated from the seeds of the plant Crambe abyssinica, as a model for NMR investigations of membrane-associated proteins. We produced isotopically labeled crambin(P22,L25) (variant of crambin containing Pro22 and Leu25) as a cleavable fusion with staphylococcal nuclease and refolded the protein by an approach that has proved successful for the production of proteins with multiple disulfide bonds. We used NMR spectroscopy to determine the three-dimensional structure of the protein in two membrane-mimetic environments: in a mixed aqueous-organic solvent (75%/25%, acetone/water) and in DPC micelles. With the sample in the mixed solvent, it was possible to determine (&gt;NH...OC&lt;) hydrogen bonds directly by the detection of (h3)J(NC)' couplings. H-bonds determined in this manner were utilized in the refinement of the NMR-derived protein structures. With the protein in DPC (dodecylphosphocholine) micelles, we used manganous ion as an aqueous paramagnetic probe to determine the surface of crambin that is shielded by the detergent. With the exception of the aqueous solvent exposed loop containing residues 20 and 21, the protein surface was protected by DPC. This suggests that the protein may be similarly embedded in physiological membranes. The strategy described here for the expression and structure determination of crambin should be applicable to structural and functional studies of membrane active toxins and small membrane proteins.
-===Water refined solution structure of crambin in ACETONE/WATER===
+Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface.,Ahn HC, Juranic N, Macura S, Markley JL J Am Chem Soc. 2006 Apr 5;128(13):4398-404. PMID:16569017<ref>PMID:16569017</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_16569017}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2eyb" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16569017 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16569017}}
+__TOC__
+</StructureSection>
-==About this Structure==
-EYB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EYB OCA].
-==Reference==
-Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface., Ahn HC, Juranic N, Macura S, Markley JL, J Am Chem Soc. 2006 Apr 5;128(13):4398-404. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16569017 16569017]
 [[Category: Crambe hispanica subsp. abyssinica]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Ahn, H C.]]
+[[Category: Ahn HC]]
-[[Category: Markley, J L.]]
+[[Category: Markley JL]]
-[[Category: Crambin]]
-[[Category: Mixed organic/aqueous solvent]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:06:04 2008''