6idc: Difference between revisions

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

OCA

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-'''Unreleased structure'''
-The entry 6idc is ON HOLD
+==Loop deletion and proline insertion mutant (deleting six residues and inserted six proline residues)==
+<StructureSection load='6idc' size='340' side='right'caption='[[6idc]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6idc]] 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=6IDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IDC 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]] 2.007&#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=6idc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6idc OCA], [https://pdbe.org/6idc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6idc RCSB], [https://www.ebi.ac.uk/pdbsum/6idc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6idc 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6idc" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Outer surface protein|Outer surface protein]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Borreliella burgdorferi]]
+[[Category: Large Structures]]
+[[Category: Makabe K]]
+[[Category: Shiga S]]