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. / text
| Identifer | oai:union.ndltd.org:UTEXAS/oai:repositories.lib.utexas.edu:2152/ETD-UT-2011-08-4330 |
| Date | 02 November 2011 |
| Creators | Meng, Qingchao, master of arts in cell and molecular biology |
| Source Sets | University of Texas |
| Language | English |
| Detected Language | English |
| Type | thesis |
| Format | application/pdf |
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