Helical Contributions Mediate Light-Activated Conformational Change in the LOV2 Domain of
Journal
ACS omega
ISSN: 2470-1343
Titre abrégé: ACS Omega
Pays: United States
ID NLM: 101691658
Informations de publication
Date de publication:
31 Jan 2019
31 Jan 2019
Historique:
received:
19
10
2018
accepted:
02
01
2019
entrez:
29
8
2019
pubmed:
29
8
2019
medline:
29
8
2019
Statut:
epublish
Résumé
Algae, plants, bacteria, and fungi contain flavin-binding light-oxygen-voltage (LOV) domains that function as blue light sensors to control cellular responses to light. In the second LOV domain of phototropins, called LOV2 domains, blue light illumination leads to covalent bond formation between protein and flavin that induces the dissociation and unfolding of a C-terminally attached α helix (Jα) and the N-terminal helix (A'α). To date, the majority of studies on these domains have focused on versions that contain truncations in the termini, which creates difficulties when extrapolating to the much larger proteins that contain these domains. Here, we study the influence of deletions and extensions of the A'α helix of the LOV2 domain of
Identifiants
pubmed: 31459397
doi: 10.1021/acsomega.8b02872
pmc: PMC6648828
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1238-1243Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM055694
Pays : United States
Déclaration de conflit d'intérêts
The authors declare no competing financial interest.
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