3TC3

Crystal Structure of SacUVDE

Summary for 3TC3

• Entry DOI: 10.2210/pdb3tc3/pdb
• Descriptor: UV damage endonuclease, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: tim-barrel, endonuclease, hydrolase
• Biological source: Sulfolobus acidocaldarius
• Total number of polymer chains: 2
• Total formula weight: 71507.45

Authors

Meulenbroek, E.M.,Jala, I.,Moolenaar, G.F.,Goosen, N.,Pannu, N.S. (deposition date: 2011-08-08, release date: 2012-11-07, Last modification date: 2024-11-06)

Primary citation

Meulenbroek, E.M.,Peron Cane, C.,Jala, I.,Iwai, S.,Moolenaar, G.F.,Goosen, N.,Pannu, N.S.
UV damage endonuclease employs a novel dual-dinucleotide flipping mechanism to recognize different DNA lesions.
Nucleic Acids Res., 41:1363-1371, 2013

PubMed Abstract: Repairing damaged DNA is essential for an organism's survival. UV damage endonuclease (UVDE) is a DNA-repair enzyme that can recognize and incise different types of damaged DNA. We present the structure of Sulfolobus acidocaldarius UVDE on its own and in a pre-catalytic complex with UV-damaged DNA containing a 6-4 photoproduct showing a novel 'dual dinucleotide flip' mechanism for recognition of damaged dipyrimidines: the two purines opposite to the damaged pyrimidine bases are flipped into a dipurine-specific pocket, while the damaged bases are also flipped into another cleft.

PubMed: 23221644
DOI: 10.1093/nar/gks1127

Experimental method

X-RAY DIFFRACTION (1.5 Å)