5lst
Crystal structure of the human RecQL4 helicase.Crystal structure of the human RecQL4 helicase.
Structural highlights
DiseaseRECQ4_HUMAN RAPADILINO syndrome;Baller-Gerold syndrome;Rothmund-Thomson syndrome type 2. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. FunctionRECQ4_HUMAN DNA-dependent ATPase. May modulate chromosome segregation.[1] Publication Abstract from PubMedRecQ4 is a member of the RecQ helicase family, an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair and replication. While reduced RecQ4 activity is associated with cancer predisposition and premature aging, RecQ4 upregulation is related to carcinogenesis and metastasis. Within the RecQ family, RecQ4 assumes an exceptional position, lacking several characteristic RecQ domains. Here we present the crystal structure of human RecQ4, encompassing the conserved ATPase core and a novel C-terminal domain that lacks resemblance to the RQC domain observed in other RecQ helicases. The new domain features a zinc-binding site and two distinct types of winged-helix domains, which are not involved in canonical DNA binding or helicase activity. Based on our structural and functional analysis, we propose that RecQ4 exerts a helicase mechanism, which may be more closely related to bacterial RecQ helicases than to its human family members. The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism.,Kaiser S, Sauer F, Kisker C Nat Commun. 2017 Jun 27;8:15907. doi: 10.1038/ncomms15907. PMID:28653661[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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