4.5 Article

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

Journal

FEBS LETTERS
Volume 594, Issue 4, Pages 740-750

Publisher

WILEY
DOI: 10.1002/1873-3468.13657

Keywords

Ap-phr; CRY-DASH; crystal structure; enzyme activity; MTHF

Funding

  1. Chinese National Natural Science Foundation [U1732114, 31971124, 31770788, U1932120, 31770895]
  2. National Key Research and Development Program of China [2017YFA0503600]

Ask authors/readers for more resources

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 angstrom 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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available