2fkj: Difference between revisions

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 <StructureSection load='2fkj' size='340' side='right'caption='[[2fkj]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2fkj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35210 Atcc 35210]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FKJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2fkj]] is a 3 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=2FKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FKJ FirstGlance]. <br>
-</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=2fkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkj OCA], [https://pdbe.org/2fkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkj RCSB], [https://www.ebi.ac.uk/pdbsum/2fkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkj ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#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=2fkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkj OCA], [https://pdbe.org/2fkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkj RCSB], [https://www.ebi.ac.uk/pdbsum/2fkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkj ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=2fkj 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.
-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 2fkj" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Outer surface protein|Outer surface protein]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 35210]]
+[[Category: Borreliella burgdorferi]]
 [[Category: Large Structures]]
-[[Category: Gawlak, G]]
+[[Category: Gawlak G]]
-[[Category: Koide, S]]
+[[Category: Koide S]]
-[[Category: Makabe, K]]
+[[Category: Makabe K]]
-[[Category: Terechko, V]]
+[[Category: Terechko V]]
-[[Category: Yan, S]]
+[[Category: Yan S]]
-[[Category: Beta sheet]]
-[[Category: De novo protein]]