2oy7: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2oy7.jpg|left|200px]]<br /><applet load="2oy7" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2oy7, resolution 1.55&Aring;" />
-'''The crystal structure of OspA mutant'''<br />
-==About this Structure==
+==The crystal structure of OspA mutant==
-OY7 is a [http://en.wikipedia.org/wiki/Single_protein 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=2OY7 OCA].
+<StructureSection load='2oy7' size='340' side='right'caption='[[2oy7]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
-[[Category: Borrelia burgdorferi]]
+== Structural highlights ==
-[[Category: Single protein]]
+<table><tr><td colspan='2'>[[2oy7]] 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=2OY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OY7 FirstGlance]. <br>
-[[Category: Koide, A.]]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
-[[Category: Koide, S.]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oy7 OCA], [https://pdbe.org/2oy7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oy7 RCSB], [https://www.ebi.ac.uk/pdbsum/2oy7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oy7 ProSAT]</span></td></tr>
-[[Category: Makabe, K.]]
+</table>
-[[Category: Terechko, V.]]
+== Function ==
-[[Category: beta-sheet]]
+[https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU]
-[[Category: membrane protein]]
+== 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/2oy7_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=2oy7 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.
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar  5 13:21:24 2008''
+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 2oy7" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Outer surface protein|Outer surface protein]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Borreliella burgdorferi]]
+[[Category: Large Structures]]
+[[Category: Koide A]]
+[[Category: Koide S]]
+[[Category: Makabe K]]
+[[Category: Terechko V]]