1jih: Difference between revisions
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'''Yeast DNA Polymerase ETA''' | '''Yeast DNA Polymerase ETA''' | ||
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[[Category: Prakash, S.]] | [[Category: Prakash, S.]] | ||
[[Category: Trincao, J.]] | [[Category: Trincao, J.]] | ||
[[Category: | [[Category: Dna polymerase]] | ||
[[Category: | [[Category: Translesion]] | ||
[[Category: | [[Category: Yeast]] | ||
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Revision as of 21:15, 2 May 2008
Yeast DNA Polymerase ETA
OverviewOverview
DNA polymerase eta is unique among eukaryotic polymerases in its proficient ability to replicate through a variety of distorting DNA lesions. We report here the crystal structure of the catalytic core of S. cerevisiae DNA polymerase eta, determined at 2.25A resolution. The structure reveals a novel polydactyl right hand-shaped molecule with a unique polymerase-associated domain. We identify the catalytic residues and show that the fingers and thumb domains are unusually small and stubby. In particular, the unexpected absence of helices "O" and "O1" in the fingers domain suggests that openness of the active site is the critical feature which enables DNA polymerase eta to replicate through DNA lesions such as a UV-induced cis-syn thymine-thymine dimer.
About this StructureAbout this Structure
1JIH is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the catalytic core of S. cerevisiae DNA polymerase eta: implications for translesion DNA synthesis., Trincao J, Johnson RE, Escalante CR, Prakash S, Prakash L, Aggarwal AK, Mol Cell. 2001 Aug;8(2):417-26. PMID:11545743 Page seeded by OCA on Fri May 2 21:15:50 2008