1z8s

Publication Abstract from PubMed

The helicase-primase interaction is a critical event in DNA replication and is mediated by a putative helicase-interaction domain within the primase. The solution structure of the helicase-interaction domain of DnaG reveals that it is made up of two independent subdomains: an N-terminal six-helix module and a C-terminal two-helix module that contains the residues of the primase previously identified as important in the interaction with the helicase. We show that the two-helix module alone is sufficient for strong binding between the primase and the helicase but fails to activate the helicase; both subdomains are required for helicase activation. The six-helix module of the primase has only one close structural homolog, the N-terminal domain of the corresponding helicase. This surprising structural relationship, coupled with the differences in surface properties of the two molecules, suggests how the helicase-interaction domain may perturb the structure of the helicase and lead to activation.

Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.,Syson K, Thirlway J, Hounslow AM, Soultanas P, Waltho JP Structure. 2005 Apr;13(4):609-16. PMID:15837199^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.