Approaching the crystal structure of the polymerase γ catalytic complex

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Approaching the crystal structure of the polymerase γ catalytic complex

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Title: Approaching the crystal structure of the polymerase γ catalytic complex
Author: Meng, Qingchao, master of arts in cell and molecular biology
Abstract: In this thesis, a 4.7Å crystal structure of the human mitochondria DNA polymerase γ catalytic complex is reported. Though the DNA substrate-binding site is not identifiable in the structure, two conformational changes in the enzyme architecture are described: 1) rotation of the distal monomer of the accessory subunit towards the catalytic subunit, and 2) shift of the thumb motif of the polymerase domain towards the active site. Both conformational changes suggest a structure of Pol γ in the DNA-bound state and in its active site “closed” conformation.
Department: Cellular and Molecular Biology
Subject: Pol γ Crystal structure Catalytic complex Polymerase γ Pol gamma Polymerase gamma Human mitochondria DNA polymerase gamma DNA DNA binding site Human mitochondria DNA polymerase γ
URI: http://hdl.handle.net/2152/ETD-UT-2011-08-4330
Date: 2011-08

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