2fkg: Difference between revisions

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-[[Image:2fkg.gif|left|200px]]<br /><applet load="2fkg" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2fkg, resolution 2.40&Aring;" />
-'''The Crystal Structure of Engineered OspA'''<br />
-==Overview==
+==The Crystal Structure of Engineered OspA==
-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.
+<StructureSection load='2fkg' size='340' side='right'caption='[[2fkg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2fkg]] 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=2FKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FKG FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#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=2fkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkg OCA], [https://pdbe.org/2fkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkg RCSB], [https://www.ebi.ac.uk/pdbsum/2fkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkg ProSAT]</span></td></tr>
+</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/fk/2fkg_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=2fkg ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FKG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of 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=2FKG OCA].
+*[[Outer surface protein|Outer surface protein]]
+__TOC__
-==Reference==
+</StructureSection>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17093048 17093048]
+[[Category: Borreliella burgdorferi]]
-[[Category: Borrelia burgdorferi]]
+[[Category: Large Structures]]
-[[Category: Protein complex]]
+[[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:42:13 2008''