Tracking the ATP-binding response in adenylate kinase in real time

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Tracking the ATP-binding response in adenylate kinase in real time. / Orädd, Fredrik; Ravishankar, Harsha; Goodman, Jack; Rogne, Per; Backman, Lars; Duelli, Annette; Pedersen, Martin Nors; Levantino, Matteo; Wulff, Michael; Wolf-Watz, Magnus; Andersson, Magnus.

In: Science Advances, Vol. 7, No. 47, eabi5514, 2021, p. 1-13.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Orädd, F, Ravishankar, H, Goodman, J, Rogne, P, Backman, L, Duelli, A, Pedersen, MN, Levantino, M, Wulff, M, Wolf-Watz, M & Andersson, M 2021, 'Tracking the ATP-binding response in adenylate kinase in real time', Science Advances, vol. 7, no. 47, eabi5514, pp. 1-13. https://doi.org/10.1126/sciadv.abi5514

APA

Orädd, F., Ravishankar, H., Goodman, J., Rogne, P., Backman, L., Duelli, A., Pedersen, M. N., Levantino, M., Wulff, M., Wolf-Watz, M., & Andersson, M. (2021). Tracking the ATP-binding response in adenylate kinase in real time. Science Advances, 7(47), 1-13. [eabi5514]. https://doi.org/10.1126/sciadv.abi5514

Vancouver

Orädd F, Ravishankar H, Goodman J, Rogne P, Backman L, Duelli A et al. Tracking the ATP-binding response in adenylate kinase in real time. Science Advances. 2021;7(47):1-13. eabi5514. https://doi.org/10.1126/sciadv.abi5514

Author

Orädd, Fredrik ; Ravishankar, Harsha ; Goodman, Jack ; Rogne, Per ; Backman, Lars ; Duelli, Annette ; Pedersen, Martin Nors ; Levantino, Matteo ; Wulff, Michael ; Wolf-Watz, Magnus ; Andersson, Magnus. / Tracking the ATP-binding response in adenylate kinase in real time. In: Science Advances. 2021 ; Vol. 7, No. 47. pp. 1-13.

Bibtex

@article{1c5770a8e3ba4ffa9f7baf0f503dfbd4,
title = "Tracking the ATP-binding response in adenylate kinase in real time",
abstract = "The biological function of proteins is critically dependent on dynamics inherent to the native structure. Such structural dynamics obey a predefined order and temporal timing to execute the specific reaction. Determination of the cooperativity of key structural rearrangements requires monitoring protein reactions in real time. In this work, we used time-resolved x-ray solution scattering (TR-XSS) to visualize structural changes in the Escherichia coli adenylate kinase (AdK) enzyme upon laser-induced activation of a protected ATP substrate. A 4.3-ms transient intermediate showed partial closing of both the ATP- and AMP-binding domains, which indicates a cooperative closing mechanism. The ATP-binding domain also showed local unfolding and breaking of an Arg131-Asp146 salt bridge. Nuclear magnetic resonance spectroscopy data identified similar unfolding in an Arg131Ala AdK mutant, which refolded in a closed, substrate-binding conformation. The observed structural dynamics agree with a {"}cracking mechanism{"} proposed to underlie global structural transformation, such as allostery, in proteins.",
author = "Fredrik Or{\"a}dd and Harsha Ravishankar and Jack Goodman and Per Rogne and Lars Backman and Annette Duelli and Pedersen, {Martin Nors} and Matteo Levantino and Michael Wulff and Magnus Wolf-Watz and Magnus Andersson",
year = "2021",
doi = "10.1126/sciadv.abi5514",
language = "English",
volume = "7",
pages = "1--13",
journal = "Science advances",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "47",

}

RIS

TY - JOUR

T1 - Tracking the ATP-binding response in adenylate kinase in real time

AU - Orädd, Fredrik

AU - Ravishankar, Harsha

AU - Goodman, Jack

AU - Rogne, Per

AU - Backman, Lars

AU - Duelli, Annette

AU - Pedersen, Martin Nors

AU - Levantino, Matteo

AU - Wulff, Michael

AU - Wolf-Watz, Magnus

AU - Andersson, Magnus

PY - 2021

Y1 - 2021

N2 - The biological function of proteins is critically dependent on dynamics inherent to the native structure. Such structural dynamics obey a predefined order and temporal timing to execute the specific reaction. Determination of the cooperativity of key structural rearrangements requires monitoring protein reactions in real time. In this work, we used time-resolved x-ray solution scattering (TR-XSS) to visualize structural changes in the Escherichia coli adenylate kinase (AdK) enzyme upon laser-induced activation of a protected ATP substrate. A 4.3-ms transient intermediate showed partial closing of both the ATP- and AMP-binding domains, which indicates a cooperative closing mechanism. The ATP-binding domain also showed local unfolding and breaking of an Arg131-Asp146 salt bridge. Nuclear magnetic resonance spectroscopy data identified similar unfolding in an Arg131Ala AdK mutant, which refolded in a closed, substrate-binding conformation. The observed structural dynamics agree with a "cracking mechanism" proposed to underlie global structural transformation, such as allostery, in proteins.

AB - The biological function of proteins is critically dependent on dynamics inherent to the native structure. Such structural dynamics obey a predefined order and temporal timing to execute the specific reaction. Determination of the cooperativity of key structural rearrangements requires monitoring protein reactions in real time. In this work, we used time-resolved x-ray solution scattering (TR-XSS) to visualize structural changes in the Escherichia coli adenylate kinase (AdK) enzyme upon laser-induced activation of a protected ATP substrate. A 4.3-ms transient intermediate showed partial closing of both the ATP- and AMP-binding domains, which indicates a cooperative closing mechanism. The ATP-binding domain also showed local unfolding and breaking of an Arg131-Asp146 salt bridge. Nuclear magnetic resonance spectroscopy data identified similar unfolding in an Arg131Ala AdK mutant, which refolded in a closed, substrate-binding conformation. The observed structural dynamics agree with a "cracking mechanism" proposed to underlie global structural transformation, such as allostery, in proteins.

UR - http://www.scopus.com/inward/record.url?scp=85119418495&partnerID=8YFLogxK

U2 - 10.1126/sciadv.abi5514

DO - 10.1126/sciadv.abi5514

M3 - Journal article

C2 - 34788091

AN - SCOPUS:85119418495

VL - 7

SP - 1

EP - 13

JO - Science advances

JF - Science advances

SN - 2375-2548

IS - 47

M1 - eabi5514

ER -

ID: 286012016