A newly identified photolyase from Arthrospira platensis possesses a unique methenyltetrahydrofolate chromophore‐binding pattern

A newly identified photolyase from Arthrospira platensis possesses a unique methenyltetrahydrofolate chromophore‐binding pattern

Cyclobutane pyrimidine dimers (CPD), as a common DNA damage caused by UV radiation, often lead to skin cancer. Here, we identified a photolyase from the alga Arthrospira platensis (designated as Ap‐phr), which has been regarded as a safe organism for humans for centuries, that can efficiently repair...

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Bibliographic Details
Published in:FEBS letters Vol. 594; no. 4; pp. 740 - 750
Main Authors: Yan, Hui, Zhu, Kongfu, Teng, Maikun, Li, Xu
Format: Journal Article
Language:English
Published: England 01-02-2020
Subjects:
Ap‐phr
crystal structure
CRY‐DASH
enzyme activity
MTHF
crystal structure
MTHF
CRY-DASH
enzyme activity
Ap-phr
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Summary:Cyclobutane pyrimidine dimers (CPD), as a common DNA damage caused by UV radiation, often lead to skin cancer. Here, we identified a photolyase from the alga Arthrospira platensis (designated as Ap‐phr), which has been regarded as a safe organism for humans for centuries, that can efficiently repair CPD lesions in ssDNA and dsDNA in vitro. The 1.6 Å resolution crystal structure of Ap‐phr revealed that it possesses a unique methenyltetrahydrofolate chromophore‐binding pattern with high energy transfer efficiency. Our study of Ap‐phr highlights its potential use in cosmetic, industrial and aesthetic medicine applications.
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ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.13657