1Z8S

DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)

Summary for 1Z8S

• Entry DOI: 10.2210/pdb1z8s/pdb
• NMR Information: BMRB: 6716
• Descriptor: DNA primase (1 entity in total)
• Functional Keywords: two alpha helical sub-domains, transferase
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 1
• Total formula weight: 16846.58

Authors

Syson, K.,Thirlway, J.,Hounslow, A.M.,Soultanas, P.,Waltho, J.P. (deposition date: 2005-03-31, release date: 2005-10-04, Last modification date: 2024-05-22)

Primary citation

Syson, K.,Thirlway, J.,Hounslow, A.M.,Soultanas, P.,Waltho, J.P.
Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation
Structure, 13:609-616, 2005

PubMed Abstract: 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.

PubMed: 15837199
DOI: 10.1016/j.str.2005.01.0220.1016

Experimental method

SOLUTION NMR