Allostery at a Protein-Protein Interface Harboring an Intermolecular Motional Network

被引:0
|
作者
Medina Gomez, Sara [1 ]
Gonzalez, Tye I. [1 ]
Vasa, Suresh K. [1 ]
Linser, Rasmus [1 ]
机构
[1] TU Dortmund Univ, Dept Chem & Chem Biol, Otto Hahn Str 4a, D-44227 Dortmund, Germany
基金
欧洲研究理事会;
关键词
Solid-state NMR spectroscopy; Protein dynamics; Dynamic networks; Allostery; DYNAMICS;
D O I
10.1002/anie.202411472
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Motional properties of proteins govern recognition, catalysis, and regulation. The dynamics of tightly interacting residues can form intramolecular dynamic networks, dependencies fine-tuned by evolution to optimize a plethora of functional aspects. The constructive interaction of residues from different proteins to assemble intermolecular dynamic networks is a similarly likely case but has escaped thorough experimental assessment due to interfering association/dissociation dynamics. Here, we use fast-MAS solid-state 15N R1 rho NMR relaxation dispersion aided by molecular-dynamics simulations to mechanistically assess the hierarchy of individual mu s timescale motions arising from a crystal-crystal contact, in the absence of translational motion. In contrast to the monomer, where particular mutations entail isolated perturbations, specific intermolecular interactions couple the motional properties between distant residues in the same protein. The mechanistic insights obtained from this conceptual work may improve our understanding on how intramolecular allostery can be tuned by intermolecular interactions via assembly of dynamic networks from previously isolated elements. Intramolecular dynamic networks allow for regulation of protein function by dynamic allostery, but it has been unclear whether such networks can be positively modulated through protein-protein association. It is now shown that the formation of a protein-protein interface can motionally couple distant sites, turning preexisting structures into functional networks. image
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页数:6
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