File:Shared primase-binding peptide in archaeal PolD and eukaryotic Polα.pdf
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Summary[edit]
| Summary | |
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| Description | a Structural comparison of the Pyrococcus abyssi PolD DP1-DP2(1093–1216) region of the cryo-EM structure with the Homo sapiens Polα POLA2-POLA1(1319–1456) crystal structure (PDB ID: 5EXR). b Shared structural features between archaeal PolD and eukaryotic Polα C-terminal regions. Conserved α-helices and Zn-binding domain are shown in blue and green, respectively. c The cPIP of DP2 resembles the primase-interacting motif located in the C terminus of Polα. Top panel: multiple-sequence alignment highlighting the conservation between the PolD cPIP motifs from Thermococcus species and the primase-interacting peptides of Polα. Sequence similarities are highlighted with light purple boxes, whereas conserved residues are shown with dark purple boxes. Bottom panel: superimposition of the X-ray crystal structures of the cPIP from P. abyssi and the primase-interacting peptide of H. sapiens Polα (PDB ID: 5EXR). Cα-traces are represented as ball and sticks. Conserved residues are highlighted using larger spheres. |
| Source | Wikimedia Commons file page |
| Author | Clément Madru, Ghislaine Henneke, Pierre Raia, Inès Hugonneau-Beaufet, Gérard Pehau-Arnaudet, Patrick England, Erik Lindahl, Marc Delarue, Marta Carroni & Ludovic Sauguet |
| Permission | See original Commons license details. |
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Original attribution and file history: Wikimedia Commons
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