Crystal structure and molecular mechanism of an E/F type bilin lyase-isomerase.
Bilin lyase
crystal structure
isomerase
photosynthesis
phycobiliprotein biogenesis
stereoselectivity
Journal
Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697
Informations de publication
Date de publication:
07 04 2022
07 04 2022
Historique:
received:
10
09
2021
revised:
01
12
2021
accepted:
17
01
2022
pubmed:
13
2
2022
medline:
13
4
2022
entrez:
12
2
2022
Statut:
ppublish
Résumé
Chromophore attachment of the light-harvesting apparatus represents one of the most important post-translational modifications in photosynthetic cyanobacteria. Extensive pigment diversity of cyanobacteria critically depends on bilin lyases that covalently attach chemically distinct chromophores to phycobiliproteins. However, how bilin lyases catalyze bilin ligation reactions and how some lyases acquire additional isomerase abilities remain elusive at the molecular level. Here, we report the crystal structure of a representative bilin lyase-isomerase MpeQ. This structure has revealed a "question-mark" protein architecture that unambiguously establishes the active site conserved among the E/F-type bilin lyases. Based on structural, mutational, and modeling data, we demonstrate that stereoselectivity of the active site plays a critical role in conferring the isomerase activity of MpeQ. We further advance a tyrosine-mediated reaction scheme unifying different types of bilin lyases. These results suggest that lyases and isomerase actions of bilin lyases arise from two coupled molecular events of distinct origin.
Identifiants
pubmed: 35148828
pii: S0969-2126(22)00007-7
doi: 10.1016/j.str.2022.01.007
pmc: PMC8995348
mid: NIHMS1778566
pii:
doi:
Substances chimiques
Bile Pigments
0
Phycobiliproteins
0
Lyases
EC 4.-
Isomerases
EC 5.-
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
564-574.e3Subventions
Organisme : NEI NIH HHS
ID : R01 EY024363
Pays : United States
Commentaires et corrections
Type : CommentIn
Informations de copyright
Copyright © 2022 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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