7fjr: Difference between revisions
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==Structure of a mutant of OspA== | |||
<StructureSection load='7fjr' size='340' side='right'caption='[[7fjr]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7fjr]] 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=7FJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FJR 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]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=7fjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fjr OCA], [https://pdbe.org/7fjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fjr RCSB], [https://www.ebi.ac.uk/pdbsum/7fjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fjr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/OSPA_BORBU OSPA_BORBU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Domain swapping is a process wherein a portion of a protein is exchanged with its counterpart in another copy of the molecule, resulting in the formation of homo-oligomers with concomitant repacking of a hydrophobic core. Here, we report domain swapping triggered upon modifying a beta-hairpin sequence within a single-layer beta-sheet (SLB) of a model protein, OspA that did not involve the formation of a reorganized hydrophobic core. The replacement of two beta-hairpin sequences with a Gly-Gly and shorteing of a beta-hairpin resulted in a protein that formed two distinct crystal structures under similar conditions: one was monomeric, similar to the parental molecule, whereas the other was a domain-swapped dimer, mediated by an intermolecular beta-sheet in the SLB portion. Based on the dimer interface structure, we replaced the Gly-Gly sequence with three-residue sequences that enable the formation of a consecutive intermolecular beta-sheet, including the Cys-Thr-Cys sequence that formed a stable disulfide-linked dimer. These results provide new insights into protein folding, evolution, and the designability of protein structure. | |||
beta-Strand-mediated Domain-swapping in the Absence of Hydrophobic Core Repacking.,Kiya M, Shiga S, Ding P, Koide S, Makabe K J Mol Biol. 2024 Jan 15;436(2):168405. doi: 10.1016/j.jmb.2023.168405. Epub 2023 , Dec 15. PMID:38104859<ref>PMID:38104859</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7fjr" 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 09:17, 21 November 2024
Structure of a mutant of OspAStructure of a mutant of OspA
Structural highlights
FunctionPublication Abstract from PubMedDomain swapping is a process wherein a portion of a protein is exchanged with its counterpart in another copy of the molecule, resulting in the formation of homo-oligomers with concomitant repacking of a hydrophobic core. Here, we report domain swapping triggered upon modifying a beta-hairpin sequence within a single-layer beta-sheet (SLB) of a model protein, OspA that did not involve the formation of a reorganized hydrophobic core. The replacement of two beta-hairpin sequences with a Gly-Gly and shorteing of a beta-hairpin resulted in a protein that formed two distinct crystal structures under similar conditions: one was monomeric, similar to the parental molecule, whereas the other was a domain-swapped dimer, mediated by an intermolecular beta-sheet in the SLB portion. Based on the dimer interface structure, we replaced the Gly-Gly sequence with three-residue sequences that enable the formation of a consecutive intermolecular beta-sheet, including the Cys-Thr-Cys sequence that formed a stable disulfide-linked dimer. These results provide new insights into protein folding, evolution, and the designability of protein structure. beta-Strand-mediated Domain-swapping in the Absence of Hydrophobic Core Repacking.,Kiya M, Shiga S, Ding P, Koide S, Makabe K J Mol Biol. 2024 Jan 15;436(2):168405. doi: 10.1016/j.jmb.2023.168405. Epub 2023 , Dec 15. PMID:38104859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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