Literature summary for 4.1.99.3 extracted from

Brolich, M.A.; Wang, L.; ONeill, M.A.
Folding kinetics of recognition loop peptides from a photolyase and cryptochrome-DASH (2010), Biochem. Biophys. Res. Commun., 391, 874-878.

Search for more literature for 4.1.99.3

Organism

Organism	UniProt	Comment	Textmining
Synechococcus elongatus PCC 7942 = FACHB-805	-	-	-

Synonyms

Synonyms	Comment	Organism
photolyase	-	Synechococcus elongatus PCC 7942 = FACHB-805

General Information

General Information	Comment	Organism
physiological function	photolyase can repair UV-damaged DNA in a mechanism requiring light and DNA base flipping, whereas cytochromes cannot repair DNA. Evolution of loop sequence likely plays a key role in functional diversification of cryptochromes and photolyases, through tuning of substrate recognition. Cryptochrome-DASH recognition loop peptide folds 2.5fold faster than its counterpart in photolyase, predominantly due to a lower enthalpy of activation. Binding duplex DNA in the catalytically-active base-flipped conformation imposes significant order on the recognition loop, and a corresponding entropic penalty, which may be surmounted by the more preorganized photolyase recognition loop, but may impose too large a barrier for the more dynamic loop in cryptochrome-DASH	Synechococcus elongatus PCC 7942 = FACHB-805

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Release 2023.1 (January 2023)