View source for 9fzm


==helix shuffled variant of domain B pf protein A==
<StructureSection load='9fzm' size='340' side='right'caption='[[9fzm]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9fzm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FZM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=9fzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fzm OCA], [https://pdbe.org/9fzm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fzm RCSB], [https://www.ebi.ac.uk/pdbsum/9fzm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fzm ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The B domain of protein A is a biotechnologically important three-helix bundle protein. It binds the Fc fragment of antibodies with helix 1/2 and the Fab region with helix 2/3. Here we designed a helix shuffled variant by changing the connectivity of the helices, in order to redesign the helix bundle, yielding altered helix-loop-helix properties. The new loops that generate the new connectivity were created in several protein libraries, and Fc binding variants were selected for a detailed biochemical characterization. We were able to create variants with Fc binding affinity at the same level as the wild type B but with significantly reduced thermal stability. The NMR structure proved that the overall three-dimensional structure was maintained not only in the helix shuffled variant but also points to some potential local differences to wild-type B, which could be the reason for the reduced thermal stability. Therefore, protein A is an example of an optimized structure being more important for stability than for function. Using the helix shuffled variant as a ligand on an affinity column facilitates a robust and straightforward purification of antibodies, but allows for a milder elution at less extreme pH. Therefore, the helix shuffled variant is a suitable ligand to purify more pH-sensitive antibodies.

A functional helix shuffled variant of the B domain of Staphylococcus aureus.,Bobolowski H, Fiedler E, Haupts U, Lilie H, Weininger U Protein Sci. 2025 Feb;34(2):e70012. doi: 10.1002/pro.70012. PMID:39840789<ref>PMID:39840789</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9fzm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Bobolowski H]]
[[Category: Weininger U]]