Crystal structure of the heterotrimeric PriSLX primase from S. solfataricus.

Primer synthesis by a eukaryotic-like archaeal primase is independent of its Fe-S cluster.

Chain B is an engineered polypeptide. It contains the PriL residues of a chimeric construct spanning amino acids 1 to 211 of PriL fused to amino acids 42 to 154 of PriX.
DNA primase large subunit PriL,PriL-X fusion protein

MGTFTLHQGQTNLIKSFFRNYYLNAELELPKDMELREFALQPFGSDTYVRHLSFSSSEELRDYLVNRNLPLHLFYSSARY
QLPSARNMEEKAWMGSDLLFDIDADHLCKLRSIRFCPVCGNAVVSEKCERDNVETLEYVEMTSECIKRGLEQTRNLVEIL
EDDFGLKPKVYFSGNRGFHVQVDCYGNCALLDSDERKEIAEYVMGIGVPGYPGGSENAPGWVGRKNRGINGVTIDEQVTI
DVKRLIRIPNSLHGKSGLIVKRVPNLDDFEFNETLSPFTGYTIFLPYITIETEVLGSIIKLNRGIPIKIKSSIGIYLHLR
NLGEVKAYVR

MALDVKKYPFIKSLDDELKKYGGGITLTDLLLNSTTLIDQAKDRIQKTKSGDELPHYVSYNEPVLVFYTTLLSLAILNDV
KLIRRYAYAEAKQFRSLLHTENEENLLEISKLLDLKINRCDPIKFYLEKKRRIIQKEFCVHFIDYLKYTKDLKEDWKLSG
QILHKGYVYLDKNQLIGLIAESIKSKIVEMIRPLNLKEIPEKLKSLIERRGKVEGKFPPQPKKSSDYSWIEKVLEMGLQD
SRKRFILYVASRYLVNVKGVNEDEALQTLKEFYYKLQSGKVYESWLKSVINGVKKKGLLPWSLKRIEERDKEMYNEIIRV
LKNS

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

12% PEG 3350, 200 mM CaCl2, 0.5% n-octyl-beta-D-glucoside

Primase, DNA-dependent RNA polymerase, DNA replication, REPLICATION

MALDVKKYPFIKSLDDELKKYGGGITLTDLLLNSTTLIDQAKDRIQKTKSGDELPHYVSYNEPVLVFYTTLLSLAILNDV
KLIRRYAYAEAKQFRSLLHTENEENLLEISKLLDLKINRCDPIKFYLEKKRRIIQKEFCVHFIDYLKYTKDLKEDWKLSG
QILHKGYVYLDKNQLIGLIAESIKSKIVEMIRPLNLKEIPEKLKSLIERRGIIPP