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6gvu

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NMR structure of the DNA-bound helix bundle domain from the functional pRN1 primase

Structural highlights

6gvu is a 2 chain structure with sequence from Sulfolobus islandicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q54324_SULIS

Publication Abstract from PubMed

Primases have a fundamental role in DNA replication. They synthesize a primer that is then extended by DNA polymerases. Archaeoeukaryotic primases require for synthesis a catalytic and an accessory domain, the exact contribution of the latter being unresolved. For the pRN1 archaeal primase, this domain is a 115-amino acid helix bundle domain (HBD). Our structural investigations of this small HBD by liquid- and solid-state nuclear magnetic resonance (NMR) revealed that only the HBD binds the DNA template. DNA binding becomes sequence-specific after a major allosteric change in the HBD, triggered by the binding of two nucleotide triphosphates. The spatial proximity of the two nucleotides and the DNA template in the quaternary structure of the HBD strongly suggests that this small domain brings together the substrates to prepare the first catalytic step of primer synthesis. This efficient mechanism is likely general for all archaeoeukaryotic primases.

A Small Helical Bundle Prepares Primer Synthesis by Binding Two Nucleotides that Enhance Sequence-Specific Recognition of the DNA Template.,Boudet J, Devillier JC, Wiegand T, Salmon L, Meier BH, Lipps G, Allain FH Cell. 2018 Dec 18. pii: S0092-8674(18)31556-3. doi: 10.1016/j.cell.2018.11.031. PMID:30595448^[1]

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

References

↑ Boudet J, Devillier JC, Wiegand T, Salmon L, Meier BH, Lipps G, Allain FH. A Small Helical Bundle Prepares Primer Synthesis by Binding Two Nucleotides that Enhance Sequence-Specific Recognition of the DNA Template. Cell. 2018 Dec 18. pii: S0092-8674(18)31556-3. doi: 10.1016/j.cell.2018.11.031. PMID:30595448 doi:http://dx.doi.org/10.1016/j.cell.2018.11.031