4wyh

Crystal structure of PriX from the hyperthermophilic archaeon Sulfolobus solfataricusCrystal structure of PriX from the hyperthermophilic archaeon Sulfolobus solfataricus

Structural highlights 4wyh is a 1 chain structure with sequence from Saccharolobus solfataricus P2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q97ZS7_SACS2 Publication Abstract from PubMed 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. A primase subunit essential for efficient primer synthesis by an archaeal eukaryotic-type primase.,Liu B, Ouyang S, Makarova KS, Xia Q, Zhu Y, Li Z, Guo L, Koonin EV, Liu ZJ, Huang L Nat Commun. 2015 Jun 22;6:7300. doi: 10.1038/ncomms8300. PMID:26095544 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 4wyh, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image