6XVM

Crystal structure of c-Src SH3 domain without ATCUN motif: monomer 2

6XVM の概要

• エントリーDOI: 10.2210/pdb6xvm/pdb
• 分子名称: Proto-oncogene tyrosine-protein kinase Src, GLYCEROL (3 entities in total)
• 機能のキーワード: beta barrel, sh3 domain, protein binding
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 35594.51

構造登録者

Camara-Artigas, A.,Plaza-Garrido, M. (登録日: 2020-01-22, 公開日: 2020-04-22, 最終更新日: 2024-01-24)

主引用文献

Plaza-Garrido, M.,Salinas-Garcia, M.C.,Martinez, J.C.,Camara-Artigas, A.
The effect of an engineered ATCUN motif on the structure and biophysical properties of the SH3 domain of c-Src tyrosine kinase.
J.Biol.Inorg.Chem., 25:621-634, 2020

PubMed Abstract: Metal binding to sites engineered in proteins can provide an increase in their stability and facilitate new functions. Besides the sites introduced in purpose, sometimes they are present accidentally as a consequence of the expression system used to produce the protein. This happens with the copper- and nickel-binding (ATCUN) motif generated by the amino-terminal residues Gly-Ser-His. This ATCUN motif is fortuitously present in many proteins, but how it affects the structural and biophysical characterization of the proteins has not been studied. In this work, we have compared the structure and biophysical properties of a small modular domain, the SH3 domain of the c-Src tyrosine kinase, cloned with and without an ATCUN motif at the N terminus. At pH 7.0, the SH3 domain with the ATCUN motif binds nickel with a binding constant K = 28.0 ± 3.0 mM. The formation of the nickel complex increases the thermal and chemical stability of the SH3 domain. A comparison of the crystal structures of the SH3 domain with and without the ATCUN motif shows that the binding of nickel does not affect the overall structure of the SH3 domain. In all crystal structures analyzed, residues Gly-Ser-His in complex with Ni show a square planar geometry. The CD visible spectrum of the nickel complex shows that this geometry is also present in the solution. Therefore, our results not only show that the ATCUN motif might influence the biophysical properties of the protein, but also points to an advantageous stabilization of the protein with potential biotechnological applications.

PubMed: 32279137
DOI: 10.1007/s00775-020-01785-0

実験手法

X-RAY DIFFRACTION (0.9 Å)