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  Photoactivation mechanism of a bacterial light-regulated adenylyl cyclase

Lindner, R., Hartmann, E., Tarnawski, M., Winkler, A., Frey, D., Reinstein, J., et al. (2017). Photoactivation mechanism of a bacterial light-regulated adenylyl cyclase. Journal of Molecular Biology (London), 429(9), 1336-1351. doi:10.1016/j.jmb.2017.03.020.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-298C-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-2A37-4
Genre: Journal Article

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JMolBiol_429_2017_1336.pdf (Any fulltext), 2MB
 
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 Creators:
Lindner, Robert1, Author              
Hartmann, Elisabeth1, Author              
Tarnawski, Miroslaw1, Author              
Winkler, Andreas1, Author              
Frey, Daniel1, Author              
Reinstein, Jochen1, Author              
Meinhart, Anton1, Author              
Schlichting, Ilme1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: BLUF photoreceptor; adenylyl cyclase; allosteric regulation; enzyme mechanism; structure-function relationship
 Abstract: Light-regulated enzymes enable organisms to quickly respond to changing light conditions. We characterize a photoactivatable adenylyl cyclase (AC) from Beggiatoa sp. (bPAC) that translates a blue light signal into the production of the second messenger cyclic AMP. bPAC contains a BLUF photoreceptor domain that senses blue light using a flavin chromophore, linked to an AC domain. We present a dark state crystal structure of bPAC that closely resembles the recently published structure of the homologous OaPAC from Oscillatoria acuminata. To elucidate the structural mechanism of light-dependent AC activation by the BLUF domain, we determined the crystal structures of illuminated bPAC and of a pseudo-lit state variant. We use hydrogen–deuterium exchange measurements of secondary structure dynamics and hypothesis-driven point mutations to trace the activation pathway from the chromophore in the BLUF domain to the active site of the cyclase. The structural changes are relayed from the residues interacting with the excited chromophore through a conserved kink of the BLUF β-sheet to a tongue-like extrusion of the AC domain that regulates active site opening and repositions catalytic residues. Our findings not only show the specific molecular pathway of photoactivation in BLUF-regulated ACs but also have implications for the general understanding of signaling in BLUF domains and of the activation of ACs.

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Language(s): eng - English
 Dates: 2017-03-082016-12-222017-03-172017-03-212017-05-05
 Publication Status: Published in print
 Pages: 16
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 Table of Contents: -
 Rev. Method: Peer
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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 429 (9) Sequence Number: - Start / End Page: 1336 - 1351 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042