4GLE

SacUVDE in complex with 6-4PP-containing DNA

Summary for 4GLE

• Entry DOI: 10.2210/pdb4gle/pdb
• Related: 3TC3
• Descriptor: 5'-D(*CP*GP*TP*CP*GP*TP*CP*AP*AP*GP*GP*AP*CP*GP*C)-3', 5'-D(*GP*CP*GP*TP*CP*CP*(64T)P*(5PY)P*GP*AP*CP*GP*AP*CP*G)-3', UV damage endonuclease, ... (5 entities in total)
• Functional Keywords: tim barrel, hydrolase-dna complex, hydrolase/dna
• Biological source: Sulfolobus acidocaldarius
• Total number of polymer chains: 3
• Total formula weight: 45073.89

Authors

Meulenbroek, E.M.,Peron Cane, C.,Jala, I.,Iwai, S.,Moolenaar, G.F.,Goosen, N.,Pannu, N.S. (deposition date: 2012-08-14, release date: 2012-11-21, 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 (2.7 Å)