2af5: Difference between revisions

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-{{Seed}}
-[[Image:2af5.png|left|200px]]
-<!--
+==2.5A X-ray Structure of Engineered OspA protein==
-The line below this paragraph, containing "STRUCTURE_2af5", creates the "Structure Box" on the page.
+<StructureSection load='2af5' size='340' side='right'caption='[[2af5]], [[Resolution|resolution]] 2.50&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'>[[2af5]] is a 1 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=2AF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AF5 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]] 2.5&#8491;</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=2af5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2af5 OCA], [https://pdbe.org/2af5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2af5 RCSB], [https://www.ebi.ac.uk/pdbsum/2af5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2af5 ProSAT]</span></td></tr>
-{{STRUCTURE_2af5|  PDB=2af5  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU]
+== 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/af/2af5_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=2af5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Although the beta-rich self-assemblies are a major structural class for polypeptides and the focus of intense research, little is known about their atomic structures and dynamics due to their insoluble and noncrystalline nature. We developed a protein engineering strategy that captures a self-assembly segment in a water-soluble molecule. A predefined number of self-assembling peptide units are linked, and the beta-sheet ends are capped to prevent aggregation, which yields a mono-dispersed soluble protein. We tested this strategy by using Borrelia outer surface protein (OspA) whose single-layer beta-sheet located between two globular domains consists of two beta-hairpin units and thus can be considered as a prototype of self-assembly. We constructed self-assembly mimics of different sizes and determined their atomic structures using x-ray crystallography and NMR spectroscopy. Highly regular beta-sheet geometries were maintained in these structures, and peptide units had a nearly identical conformation, supporting the concept that a peptide in the regular beta-geometry is primed for self-assembly. However, we found small but significant differences in the relative orientation between adjacent peptide units in terms of beta-sheet twist and bend, suggesting their inherent flexibility. Modeling shows how this conformational diversity, when propagated over a large number of peptide units, can lead to a substantial degree of nanoscale polymorphism of self-assemblies.
-===2.5A X-ray Structure of Engineered OspA protein===
+Atomic structures of peptide self-assembly mimics.,Makabe K, McElheny D, Tereshko V, Hilyard A, Gawlak G, Yan S, Koide A, Koide S Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17753-8. Epub 2006 Nov 8. PMID:17093048<ref>PMID:17093048</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2af5" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17093048}}, adds the Publication Abstract to the page
+*[[Outer surface protein|Outer surface protein]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17093048 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17093048}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Borreliella burgdorferi]]
-AF5 is a 1 chain structure of sequence 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=2AF5 OCA].
+[[Category: Large Structures]]
+[[Category: Hilyard A]]
-==Reference==
+[[Category: Koide A]]
-<ref group="xtra">PMID:17093048</ref><ref group="xtra">PMID:10667801</ref><references group="xtra"/>
+[[Category: Koide S]]
-[[Category: Borrelia burgdorferi]]
+[[Category: Makabe K]]
-[[Category: Hilyard, A.]]
+[[Category: Mcelheny D]]
-[[Category: Koide, A.]]
+[[Category: Tereshko V]]
-[[Category: Koide, S.]]
-[[Category: Makabe, K.]]
-[[Category: Mcelheny, D.]]
-[[Category: Tereshko, V.]]
-[[Category: Beta-hairpin]]
-[[Category: Repeat protein]]
-[[Category: Single-layer beta-sheet]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:44:46 2009''