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Tracking the ATP-bi...
Tracking the ATP-binding response in adenylate kinase in real time
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- Orädd, Fredrik (author)
- Umeå universitet,Kemiska institutionen
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- Ravishankar, Harsha (author)
- Umeå universitet,Kemiska institutionen
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- Goodman, Jack (author)
- Umeå universitet,Kemiska institutionen
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- Rogne, Per (author)
- Umeå universitet,Kemiska institutionen
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- Backman, Lars, 1951- (author)
- Umeå universitet,Kemiska institutionen
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- Duelli, Annette (author)
- Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark
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- Nors Pedersen, Martin (author)
- ESRF - The European Synchrotron, Grenoble, France
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- Levantino, Matteo (author)
- ESRF - The European Synchrotron, Grenoble, France
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- Wulff, Michael (author)
- ESRF - The European Synchrotron, Grenoble, France
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- Wolf-Watz, Magnus, 1971- (author)
- Umeå universitet,Kemiska institutionen
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- Andersson, Magnus (author)
- Umeå universitet,Kemiska institutionen
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(creator_code:org_t)
- American Association for the Advancement of Science, 2021
- 2021
- English.
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In: Science Advances. - : American Association for the Advancement of Science. - 2375-2548. ; 7:47
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Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Multidisciplinary
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Orädd, Fredrik
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Ravishankar, Har ...
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Goodman, Jack
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Rogne, Per
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Backman, Lars, 1 ...
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Duelli, Annette
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Nors Pedersen, M ...
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Levantino, Matte ...
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Wulff, Michael
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Wolf-Watz, Magnu ...
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Andersson, Magnu ...
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
- Articles in the publication
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Science Advances
- By the university
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Umeå University