3eex: Difference between revisions

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-{{Seed}}
-[[Image:3eex.png|left|200px]]
-<!--
+==The crystal structure of OspA mutant==
-The line below this paragraph, containing "STRUCTURE_3eex", creates the "Structure Box" on the page.
+<StructureSection load='3eex' size='340' side='right'caption='[[3eex]], [[Resolution|resolution]] 2.49&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'>[[3eex]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi Borreliella burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EEX 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]] 2.49&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
-{{STRUCTURE_3eex|  PDB=3eex  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eex OCA], [https://pdbe.org/3eex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eex RCSB], [https://www.ebi.ac.uk/pdbsum/3eex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eex ProSAT]</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/ee/3eex_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=3eex ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Demonstrated successes of protein design and engineering suggest significant potential to produce diverse protein architectures and assemblies beyond those found in nature. Here, we describe a new class of synthetic protein architecture through the successful design and atomic structures of water-soluble cross-beta proteins. The cross-beta motif is formed from the lamination of successive beta-sheet layers, and it is abundantly observed in the core of insoluble amyloid fibrils associated with protein-misfolding diseases. Despite its prominence, cross-beta has been designed only in the context of insoluble aggregates of peptides or proteins. Cross-beta's recalcitrance to protein engineering and conspicuous absence among the known atomic structures of natural proteins thus makes it a challenging target for design in a water-soluble form. Through comparative analysis of the cross-beta structures of fibril-forming peptides, we identified rows of hydrophobic residues ("ladders") running across beta-strands of each beta-sheet layer as a minimal component of the cross-beta motif. Grafting a single ladder of hydrophobic residues designed from the Alzheimer's amyloid-beta peptide onto a large beta-sheet protein formed a dimeric protein with a cross-beta architecture that remained water-soluble, as revealed by solution analysis and x-ray crystal structures. These results demonstrate that the cross-beta motif is a stable architecture in water-soluble polypeptides and can be readily designed. Our results provide a new route for accessing the cross-beta structure and expanding the scope of protein design.
-===The crystal structure of OspA mutant===
+Minimalist design of water-soluble cross-{beta} architecture.,Biancalana M, Makabe K, Koide S Proc Natl Acad Sci U S A. 2010 Feb 23;107(8):3469-74. Epub 2010 Feb 4. PMID:20133689<ref>PMID:20133689</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3eex" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20133689}}, adds the Publication Abstract to the page
+*[[Outer surface protein|Outer surface protein]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20133689 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20133689}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Borreliella burgdorferi]]
-EEX is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Borrelia_burgdorferi Borrelia burgdorferi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EEX OCA].
+[[Category: Large Structures]]
+[[Category: Biancalana M]]
-==Reference==
+[[Category: Koide S]]
-<ref group="xtra">PMID:20133689</ref><references group="xtra"/>
+[[Category: Makabe K]]
-[[Category: Borrelia burgdorferi]]
-[[Category: Biancalana, M.]]
-[[Category: Koide, S.]]
-[[Category: Makabe, K.]]
-[[Category: Beta-sheet]]
-[[Category: Membrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar  3 13:23:06 2010''