View source for 6iei


==Loop deletion and proline insertion mutant (deleting six residues and inserted five proline residues)==
<StructureSection load='6iei' size='340' side='right'caption='[[6iei]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6iei]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_B31 Borreliella burgdorferi B31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IEI 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=6iei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iei OCA], [https://pdbe.org/6iei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iei RCSB], [https://www.ebi.ac.uk/pdbsum/6iei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iei ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In "domain-swapping," proteins mutually interconvert structural elements to form a dimer/oligomer. Engineering this process by design is important for creating a higher order protein assembly with minimal modification. Herein, we show a simple design strategy for domain-swapping formation by loop deletion and insertion of a polyproline rod. Crystal structures revealed the formation of the domain-swapped dimers and the polyproline portion formed a polyproline II (PPII) structure. Small-angle x-ray scattering (SAXS) demonstrated that an extended orientation of domain-swapped dimer was retained in the solution. We found that a multiple of three of inserting proline residue is favored for domain-swapping because of the helical nature of PPII. The rigid nature of the polyproline rod enables precise control of the interdomain distance and orientation.

Domain-swapping design by poly-proline rod insertion.,Shiga S, Yamanaka M, Fujiwara W, Hirota S, Goda S, Makabe K Chembiochem. 2019 May 15. doi: 10.1002/cbic.201900179. PMID:31094059<ref>PMID:31094059</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iei" style="background-color:#fffaf0;"></div>

==See Also==
*[[Outer surface protein|Outer surface protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Borreliella burgdorferi B31]]
[[Category: Large Structures]]
[[Category: Makabe K]]
[[Category: Shiga S]]