3ckf
From Proteopedia
(Difference between revisions)
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| - | + | ==The crystal structure of OspA deletion mutant== | |
| - | === | + | <StructureSection load='3ckf' size='340' side='right' caption='[[3ckf]], [[Resolution|resolution]] 1.25Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3ckf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35210 Atcc 35210]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CKF FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cka|3cka]], [[3ckg|3ckg]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ospA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 ATCC 35210])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ckf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ckf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ckf RCSB], [http://www.ebi.ac.uk/pdbsum/3ckf PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/ck/3ckf_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Recent studies suggest the dominant role of main-chain H-bond formation in specifying beta-sheet topology. Its essentially sequence-independent nature implies a large degree of freedom in designing beta-sheet-based nanomaterials. Here we show rational design of beta-sheet face inversions by incremental deletions of beta-strands from the single-layer beta-sheet of Borrelia outer surface protein A. We show that a beta-sheet structure can be maintained when a large number of native contacts are removed and that one can design large-scale conformational transitions of a beta-sheet such as face inversion by exploiting the promiscuity of strand-strand interactions. High-resolution X-ray crystal structures confirmed the success of the design and supported the importance of main-chain H-bonds in determining beta-sheet topology. This work suggests a simple but effective strategy for designing and controlling nanomaterials based on beta-rich peptide self-assemblies. | ||
| - | + | The promiscuity of beta-strand pairing allows for rational design of beta-sheet face inversion.,Makabe K, Koide S J Am Chem Soc. 2008 Nov 5;130(44):14370-1. Epub 2008 Oct 9. PMID:18842042<ref>PMID:18842042</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Outer surface protein|Outer surface protein]] | *[[Outer surface protein|Outer surface protein]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Atcc 35210]] | [[Category: Atcc 35210]] | ||
[[Category: Koide, S.]] | [[Category: Koide, S.]] | ||
Revision as of 05:55, 10 October 2014
The crystal structure of OspA deletion mutant
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