2oyb: Difference between revisions

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[[Image:2oyb.jpg|left|200px]]


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==The crystal structure of OspA mutant==
The line below this paragraph, containing "STRUCTURE_2oyb", creates the "Structure Box" on the page.
<StructureSection load='2oyb' size='340' side='right'caption='[[2oyb]], [[Resolution|resolution]] 1.30&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'>[[2oyb]] 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=2OYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OYB 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]] 1.3&#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=2oyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oyb OCA], [https://pdbe.org/2oyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oyb RCSB], [https://www.ebi.ac.uk/pdbsum/2oyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oyb ProSAT]</span></td></tr>
{{STRUCTURE_2oyb|  PDB=2oyb  |  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/oy/2oyb_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=2oyb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Though beta-rich self-assemblies comprise a major structural class of polypeptides, a detailed understanding of the determinants of their structure and stability is lacking. In particular, the roles of repetitive stretches of side chains running the long axis of these beta-sheets, termed "cross-strand ladders," remain poorly characterized due to the inherently insoluble and heterogeneous nature of self-assemblies. To overcome these experimental challenges, we have established a complementary experimental system termed "peptide self-assembly mimics" (PSAMs). The PSAMs capture a defined number of self-assembly-like peptide repeats within a soluble beta-rich protein, making structural and energetic studies possible. In this work, we investigated the role of cross-strand ladders containing aromatic residues, which are prominent in self-assembling peptides. A combination of solution data and high-resolution crystal structures revealed that a single cross-strand ladder consisting solely of Tyr significantly stabilized, rigidified, and flattened the PSAM beta-sheet. These characteristics would stabilize each beta-sheet layer of a self-assembly and direct sheet conformations compatible with lamination. Our results therefore provide a rationale for the abundance of aromatic amino acids in fibril-forming peptides and establish important roles of cross-strand Tyr ladders in the structure and stability of beta-rich peptide self-assemblies.


'''The crystal structure of OspA mutant'''
Aromatic cross-strand ladders control the structure and stability of beta-rich peptide self-assembly mimics.,Biancalana M, Makabe K, Koide A, Koide S J Mol Biol. 2008 Oct 31;383(1):205-13. Epub 2008 Aug 22. PMID:18762191<ref>PMID:18762191</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2oyb" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2OYB is a [[Single protein]] 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=2OYB OCA].
*[[Outer surface protein|Outer surface protein]]
[[Category: Borrelia burgdorferi]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Biancalana, M.]]
__TOC__
[[Category: Koide, S.]]
</StructureSection>
[[Category: Makabe, K.]]
[[Category: Borreliella burgdorferi]]
[[Category: Terechko, V.]]
[[Category: Large Structures]]
[[Category: Beta-sheet]]
[[Category: Biancalana M]]
[[Category: Membrane protein]]
[[Category: Koide S]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:55:37 2008''
[[Category: Makabe K]]
[[Category: Terechko V]]
Retrieved from "https://proteopedia.org/2oyb"