Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 382, Issue 4, Pages 859-869Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.07.058
Keywords
eubacterial DNA replication; DNA polymerase III; OB-fold; ternary complex; nucleotidyltransferase
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Funding
- National Institutes of Health [GM57510]
- National Institute of General Medical Sciences [T32GM007223]
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The crystal structure of the catalytic alpha-subunit of the DNA polymerase III (PolIII alpha) holoenzyme bound to primer-template DNA and an incoming deoxy-nucleoside 5'-triphosphate has been determined at 4.6-angstrom resolution. The polymerase interacts with the sugar-phosphate backbone of the DNA across its minor groove, which is made possible by significant movements of the thumb, finger, and beta-binding domains relative to their orientations in the unliganded polymerase structure. Additionally, the DNA and incoming nucleotide are bound to the active site of PolIII alpha nearly identically as they are in their complex with DNA polymerase beta, thereby proving that the eubacterial replicating polymerase, but not the eukaryotic replicating polymerase, is homologous to DNA polymerase beta. Finally, superimposing a recent structure of the clamp bound to DNA on this PolIII alpha complex with DNA places a loop of the beta-binding domain into the appropriate clamp cleft and supports a mechanism of polymerase switching. (C) 2008 Elsevier Ltd. All rights reserved.
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