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

6NLB の概要

• エントリーDOI: 10.2210/pdb6nlb/pdb
• 分子名称: Immunoglobulin G-binding protein G, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: metal-mediated complex, b1 domain of streptococcal protein g, immunoglobulin binding protein, metal binding protein
• 由来する生物種: Streptococcus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 24984.38

構造登録者

Maniaci, B.,Stec, B.,Huxford, T. (登録日: 2019-01-08, 公開日: 2019-01-23, 最終更新日: 2023-10-25)

主引用文献

Maniaci, B.,Lipper, C.H.,Anipindi, D.L.,Erlandsen, H.,Cole, J.L.,Stec, B.,Huxford, T.,Love, J.J.
Design of High-Affinity Metal-Controlled Protein Dimers.
Biochemistry, 58:2199-2207, 2019

PubMed Abstract: 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 β1 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.

PubMed: 30938154
DOI: 10.1021/acs.biochem.9b00055

実験手法

X-RAY DIFFRACTION (2.3 Å)