1vas
From Proteopedia
|
ATOMIC MODEL OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME COMPLEXED WITH A DNA SUBSTRATE: STRUCTURAL BASIS FOR DAMAGED DNA RECOGNITION
Overview
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.
About this Structure
1VAS is a Single protein structure of sequence from Bacteriophage t4. The following page contains interesting information on the relation of 1VAS with [Thymine Dimers]. Full crystallographic information is available from OCA.
Reference
Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition., Vassylyev DG, Kashiwagi T, Mikami Y, Ariyoshi M, Iwai S, Ohtsuka E, Morikawa K, Cell. 1995 Dec 1;83(5):773-82. PMID:8521494
Page seeded by OCA on Sun Nov 18 09:06:52 2007
