Kinetic response of a photoperturbed allosteric protein

被引：87

作者：

Buchli, Brigitte ^{[1
]}

Waldauer, Steven A. ^{[1
]}

Walser, Reto ^{[1
]}

Donten, Mateusz L. ^{[1
]}

Pfister, Rolf ^{[1
]}

Bloechliger, Nicolas ^{[2
]}

Steiner, Sandra ^{[2
]}

Caflisch, Amedeo ^{[2
]}

Zerbe, Oliver ^{[1
]}

Hamm, Peter ^{[1
]}

机构：

[1] Univ Zurich, Dept Chem, CH-8057 Zurich, Switzerland

[2] Univ Zurich, Dept Biochem, CH-8057 Zurich, Switzerland

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2013年 / 110卷 / 29期

基金：

欧洲研究理事会; 瑞士国家科学基金会;

关键词：

PEPTIDE CONFORMATIONAL DYNAMICS; HUMAN PHOSPHATASE HPTP1E; PDZ DOMAIN PROTEIN; MOLECULAR-DYNAMICS; ULTRAFAST SPECTROSCOPY; SIGNALING PATHWAYS; CRYSTAL-STRUCTURE; GLASS-TRANSITION; PLAUSIBLE MODEL; PHOTO-CONTROL;

D O I：

10.1073/pnas.1306323110

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

By covalently linking an azobenzene photoswitch across the binding groove of a PDZ domain, a conformational transition, similar to the one occurring upon ligand binding to the unmodified domain, can be initiated on a picosecond timescale by a laser pulse. The protein structures have been characterized in the two photoswitch states through NMR spectroscopy and the transition between them through ultrafast IR spectroscopy and molecular dynamics simulations. The binding groove opens on a 100-ns timescale in a highly nonexponential manner, and the molecular dynamics simulations suggest that the process is governed by the rearrangement of the water network on the protein surface. We propose this rearrangement of the water network to be another possible mechanism of allostery.

引用

页码：11725 / 11730

页数：6

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