View source for 6nlb


==Crystal structure of de novo designed metal-controlled dimer of mutant B1 immunoglobulin-binding domain of Streptococcal Protein G (L12H, E15V, T16L, T18I, V29H, Y33H, N37L)-apo==
<StructureSection load='6nlb' size='340' side='right'caption='[[6nlb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nlb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/9stre 9stre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NLB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NLB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1301 9STRE])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6nlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nlb OCA], [http://pdbe.org/6nlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nlb RCSB], [http://www.ebi.ac.uk/pdbsum/6nlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nlb ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ability to precisely control protein complex formation has high utility in the expanding field of biomaterials. Driving protein-protein binding through metal-ligand bridging interactions is a promising method of achieving this goal. Furthermore, the capacity to precisely regulate both complex formation and dissociation enables additional control not available with constitutive protein complexes. Here we describe the design of three metal-controlled protein dimers that are completely monomeric in the absence of metal yet form high-affinity symmetric homodimers in the presence of zinc sulfate. The scaffold used for the designed dimers is the beta1 domain of streptococcal protein G. In addition to forming high-affinity dimers in the presence of metal, the complexes also dissociate upon addition of EDTA. Biophysical characterization revealed that the proteins maintain relatively high thermal stability, bind with high affinity, and are completely monodisperse in the monomeric and dimeric states. High-resolution crystal structures revealed that the dimers adopt the target structure and that the designed metal-binding histidine residues successfully bind zinc and function to drive dimer formation.

Design of High-Affinity Metal-Controlled Protein Dimers.,Maniaci B, Lipper CH, Anipindi DL, Erlandsen H, Cole JL, Stec B, Huxford T, Love JJ Biochemistry. 2019 Apr 30;58(17):2199-2207. doi: 10.1021/acs.biochem.9b00055., Epub 2019 Apr 12. PMID:30938154<ref>PMID:30938154</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6nlb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Huxford, T]]
[[Category: Maniaci, B]]
[[Category: B1 domain of streptococcal protein g]]
[[Category: Immunoglobulin binding protein]]
[[Category: Metal binding protein]]
[[Category: Metal-mediated complex]]