5LST
Crystal structure of the human RecQL4 helicase.
Summary for 5LST
| Entry DOI | 10.2210/pdb5lst/pdb |
| Descriptor | ATP-dependent DNA helicase Q4, ZINC ION (2 entities in total) |
| Functional Keywords | recq4, helicase, rothmund-thomson-syndrome, rapadilino-syndrome, hydrolase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm : O94761 |
| Total number of polymer chains | 1 |
| Total formula weight | 76479.17 |
| Authors | Kaiser, S.,Sauer, F.,Kisker, C. (deposition date: 2016-09-05, release date: 2017-07-05, Last modification date: 2024-05-08) |
| Primary citation | Kaiser, S.,Sauer, F.,Kisker, C. The structural and functional characterization of human RecQ4 reveals insights into its helicase mechanism. Nat Commun, 8:15907-15907, 2017 Cited by PubMed Abstract: RecQ4 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. PubMed: 28653661DOI: 10.1038/ncomms15907 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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