Structural highlights
Function
[DNAI_BACSU] Probably involved in DNA replication. [PRIM_GEOSE] DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis.
Publication Abstract from PubMed
During the assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameric helicase ring, deliver it onto the oriC DNA and then dissociate from the complex. Here, to provide a better understanding of this key process, we report the crystal structure of the ~570-kDa prepriming complex between the Bacillus subtilis loader protein and the Bacillus stearothermophilus helicase, as well as the helicase-binding domain of primase with a molar ratio of 6:6:3 at 7.5 A resolution. The overall architecture of the complex exhibits a three-layered ring conformation. Moreover, the structure combined with the proposed model suggests that the shift from the 'open-ring' to the 'open-spiral' and then the 'closed-spiral' state of the helicase ring due to the binding of single-stranded DNA may be the cause of the loader release.
Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly.,Liu B, Eliason WK, Steitz TA Nat Commun. 2013;4:2495. doi: 10.1038/ncomms3495. PMID:24048025[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu B, Eliason WK, Steitz TA. Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly. Nat Commun. 2013;4:2495. doi: 10.1038/ncomms3495. PMID:24048025 doi:10.1038/ncomms3495
