6idc: Difference between revisions
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==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]] 2.01Å' 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]] 2.007Å</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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </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]] | |||
Latest revision as of 12:37, 22 November 2023
Loop deletion and proline insertion mutant (deleting six residues and inserted six proline residues)Loop deletion and proline insertion mutant (deleting six residues and inserted six proline residues)
Structural highlights
FunctionPublication Abstract from PubMedIn "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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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