6nl8: Difference between revisions
New page: '''Unreleased structure''' The entry 6nl8 is ON HOLD Authors: Maniaci, B., Huxford, T. Description: Crystal structure of de novo designed metal-controlled dimer of mutant B1 immunoglob... |
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The | ==Crystal structure of de novo designed metal-controlled dimer of mutant B1 immunoglobulin-binding domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-zinc== | ||
<StructureSection load='6nl8' size='340' side='right'caption='[[6nl8]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6nl8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus Streptococcus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NL8 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]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6nl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nl8 OCA], [https://pdbe.org/6nl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nl8 RCSB], [https://www.ebi.ac.uk/pdbsum/6nl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nl8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Huxford | <div class="pdbe-citations 6nl8" style="background-color:#fffaf0;"></div> | ||
[[Category: Maniaci | |||
==See Also== | |||
*[[Protein G|Protein G]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus]] | |||
[[Category: Huxford T]] | |||
[[Category: Maniaci B]] | |||
[[Category: Stec B]] | |||
Latest revision as of 12:15, 25 October 2023
Crystal structure of de novo designed metal-controlled dimer of mutant B1 immunoglobulin-binding domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-zincCrystal structure of de novo designed metal-controlled dimer of mutant B1 immunoglobulin-binding domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-zinc
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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