1g5h
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CRYSTAL STRUCTURE OF THE ACCESSORY SUBUNIT OF MURINE MITOCHONDRIAL POLYMERASE GAMMA
OverviewOverview
Polymerase gamma, which replicates and repairs mitochondrial DNA, requires, the Pol gamma B subunit for processivity. We determined the crystal, structure of mouse Pol gamma B, a core component of the mitochondrial, replication machinery. Pol gamma B shows high similarity to glycyl-tRNA, synthetase and dimerizes through an unusual intermolecular four-helix, bundle. A human Pol gamma B mutant lacking the four-helix bundle failed to, dimerize in solution or to stimulate the catalytic subunit Pol gamma A, but retained the ability to bind with Pol gamma A to a primer-template, construct, indicating that the functional holoenzyme contains two Pol, gamma B molecules. Other mutants retained stimulatory activity but lost, the ability to bind folded ssDNA. These results suggest that the Pol gamma, B dimer contains distinct sites for Pol gamma A binding, dimerization, and, DNA binding.
About this StructureAbout this Structure
1G5H is a Single protein structure of sequence from Mus musculus with NA and GOL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer., Carrodeguas JA, Theis K, Bogenhagen DF, Kisker C, Mol Cell. 2001 Jan;7(1):43-54. PMID:11172710
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