Molecular Locomotion: Modeling the Functional Domains of E1 Helicase to Assess the Asymmetric Rotary Model of E1 Helicase

Autor: Michael Liapin, Simon Chigler, John Gustafson, Lily Bailey, Bowen Zhan, McClean Sherrin, Ernst ter Haar, Hansika Iyer, Judy Rokous, Nora Bradford
Rok vydání: 2015
Předmět:
Zdroj: The FASEB Journal. 29
ISSN: 1530-6860
0892-6638
Popis: Helicases are highly conserved enzymes that unwind the double helix of DNA, providing access to single-stranded DNA. Found in all living organisms and viruses, helicases function as motor proteins in replication, transcription, and remodeling of DNA. A common sexually-transmitted oncovirus, human papillomavirus (HPV) uses E1 helicase, the most studied helicase protein because of the ease by which it can be isolated. The only enzyme encoded in the HPV episome, E1 hexameric helicase is a ring-shaped translocase that belongs to the AAA+ family and superfamily 3. E1 has near exact rotational symmetry with respect to its six subunits. Each monomer comprises a central five-stranded anti-parallel beta-sheet and six alpha helices. Conserved sequence motifs Walker A and B and an arginine finger participate in the binding and hydrolysis of ATP causing conformational changes in β-hairpins, powering the walking movement along the ssDNA. Assembling first as a double-trimer at the replication origin and then into two h...
Databáze: OpenAIRE
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