1z8s
DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)
Structural highlights
FunctionDNAG_GEOSE RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. See AlsoReferences
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