1VAS

ATOMIC MODEL OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME COMPLEXED WITH A DNA SUBSTRATE: STRUCTURAL BASIS FOR DAMAGED DNA RECOGNITION

Summary for 1VAS

• Entry DOI: 10.2210/pdb1vas/pdb
• Descriptor: DNA (5'-D(*AP*TP*CP*GP*CP*GP*TP*TP*GP*CP*GP*CP*T)-3'), DNA (5'-D(*TP*AP*GP*CP*GP*CP*AP*AP*CP*GP*CP*GP*A)-3'), PROTEIN (T4 ENDONUCLEASE V (E.C.3.1.25.1)), ... (4 entities in total)
• Functional Keywords: protein-dna complex, double helix, hydrolase-dna complex, hydrolase/dna
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 3
• Total formula weight: 23916.58

Authors

Vassylyev, D.G.,Kashiwagi, T.,Mikami, Y.,Ariyoshi, M.,Iwai, S.,Ohtsuka, E.,Morikawa, K. (deposition date: 1995-09-08, release date: 1996-01-31, Last modification date: 2024-02-14)

Primary citation

Vassylyev, D.G.,Kashiwagi, T.,Mikami, Y.,Ariyoshi, M.,Iwai, S.,Ohtsuka, E.,Morikawa, K.
Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition.
Cell(Cambridge,Mass.), 83:773-782, 1995

PubMed Abstract: T4 endonuclease V is a DNA repair enzyme from bacteriophage T4 that catalyzes the first reaction step of the pyrimidine dimer-specific base excision repair pathway. The crystal structure of this enzyme complexed with a duplex DNA substrate, containing a thymine dimer, has been determined at 2.75 A resolution. The atomic structure of the complex reveals the unique conformation of the DNA duplex, which exhibits a sharp kink with a 60 degree inclination at the central thymine dimer. The adenine base complementary to the 5' side of the thymine dimer is completely flipped out of the DNA duplex and trapped in a cavity on the protein surface. These structural features allow an understanding of the catalytic mechanism and implicate a general mechanism of how other repair enzymes recognize damaged DNA duplexes.

PubMed: 8521494
DOI: 10.1016/0092-8674(95)90190-6

Experimental method

X-RAY DIFFRACTION (2.75 Å)