4WYH

Crystal structure of PriX from the hyperthermophilic archaeon Sulfolobus solfataricus

Summary for 4WYH

• Entry DOI: 10.2210/pdb4wyh/pdb
• Descriptor: Uncharacterized protein, IODIDE ION (3 entities in total)
• Functional Keywords: a novel noncatalytic subunit archaeal eukaryal-type primase, replication
• Biological source: Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
• Total number of polymer chains: 1
• Total formula weight: 15764.88

Authors

Ouyang, S. (deposition date: 2014-11-17, release date: 2015-06-24, Last modification date: 2024-03-20)

Primary citation

Liu, B.,Ouyang, S.,Makarova, K.S.,Xia, Q.,Zhu, Y.,Li, Z.,Guo, L.,Koonin, E.V.,Liu, Z.J.,Huang, L.
A primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-type primase.
Nat Commun, 6:7300-7300, 2015

PubMed Abstract: Archaea encode a eukaryotic-type primase comprising a catalytic subunit (PriS) and a noncatalytic subunit (PriL). Here we report the identification of a primase noncatalytic subunit, denoted PriX, from the hyperthermophilic archaeon Sulfolobus solfataricus. Like PriL, PriX is essential for the survival of the organism. The crystallographic analysis complemented by sensitive sequence comparisons shows that PriX is a diverged homologue of the C-terminal domain of PriL but lacks the iron-sulfur cluster. Phylogenomic analysis provides clues on the origin and evolution of PriX. PriX, PriL and PriS form a stable heterotrimer (PriSLX). Both PriSX and PriSLX show far greater affinity for nucleotide substrates and are substantially more active in primer synthesis than the PriSL heterodimer. In addition, PriL, but not PriX, facilitates primer extension by PriS. We propose that the catalytic activity of PriS is modulated through concerted interactions with the two noncatalytic subunits in primer synthesis.

PubMed: 26095544
DOI: 10.1038/ncomms8300

Experimental method

X-RAY DIFFRACTION (1.95 Å)