English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Crystal structure and mechanism of a DNA (6-4) photolyase

Maul, M. J., Barends, T., Glas, A. F., Cryle, M., Domratcheva, T., Schneider, S., et al. (2008). Crystal structure and mechanism of a DNA (6-4) photolyase. Angewandte Chemie International Edition: a journal of the Gesellschaft Deutscher Chemiker, 47(52), 10076-10080. doi:10.1002/anie.200804268.

Item is

Files

show Files
hide Files
:
AngewChem_47_2008_10076.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
AngewChem_47_2008_10076.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
AngewChem_47_2008_10076_Suppl.pdf (Supplementary material), 3MB
 
File Permalink:
-
Name:
AngewChem_47_2008_10076_Suppl.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Description:
-

Creators

show
hide
 Creators:
Maul, Melanie J., Author
Barends, Thomas1, Author              
Glas, Andreas F., Author
Cryle, Max1, Author              
Domratcheva, Tatiana1, Author              
Schneider, Sabine, Author
Schlichting, Ilme1, Author              
Carell, Thomas, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: DNA damage; DNA repair; enzymes; photochemistry; structure elucidation
 Abstract: UV irradiation of cells gives rise to the formation of cyclobutane pyrimidine dimers (CPD) and so-called (6-4) DNA lesions (Scheme 1). Both lesions are major photoproducts formed in dipyrimidine sequences of double-stranded DNA.1, 2 Repair of these lesions is essential because of their high mutagenic potential. Particularly important in many organisms are the photolyase-mediated repair systems that are able to split CPD lesions and (6-4) lesions directly back into their corresponding monomers.1, 2 While formation and photolyase repair of CPD lesions is well studied, little is known about (6-4) lesions. In particular, the mechanism of repair of the (6-4) lesions by (6-4) DNA photolyases is a long-standing question. Currently it is believed that the enzyme rearranges the (6-4) lesion with the help of two conserved histidine residues in the active site to form an oxetane intermediate (Scheme 1), which is split after single-electron donation from a light-activated FADH−.3, 4 We report here the first crystal structures of a (6-4) DNA photolyase enzyme. The structures show the enzyme in complex with a (6-4) lesion containing DNA before and after in situ repair. Based on the structural and biochemical data we propose a modified repair mechanism that lacks the strained oxetane intermediate.

Details

show
hide
Language(s): eng - English
 Dates: 2008-08-292008-10-272008-10-272008-12-15
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Angewandte Chemie International Edition : a journal of the Gesellschaft Deutscher Chemiker
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 47 (52) Sequence Number: - Start / End Page: 10076 - 10080 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/110984073528720