Structure of the human RECQ1 helicase reveals a putative strand-separation pin.
|Abstract||RecQ-like helicases, which include 5 members in the human genome, are important in maintaining genome integrity. We present a crystal structure of a truncated form of the human RECQ1 protein with Mg-ADP. The truncated protein is active in DNA fork unwinding but lacks other activities of the full-length enzyme: disruption of Holliday junctions and DNA strand annealing. The structure of human RECQ1 resembles that of Escherichia coli RecQ, with some ... [truncated at 450 characters in length]|
|Author||Pike, Ashley C W; Shrestha, Binesh; Popuri, Venkateswarlu; et al|
|Subject||Adenosine Diphosphate Adenosine Triphosphate Amino Acid Motifs Amino Acid Sequence Conserved Sequence DNA Escherichia coli Humans Kinetics Molecular Sequence Data Mutant Proteins Protein Binding Protein Structure, Tertiary RecQ Helicases Sequence Alignment Zinc metabolism metabolism enzymology chemistry chemistry metabolism metabolism|
Probing the structural basis of RecQ helicase function.
|Abstract||RecQ helicases are a ubiquitous family of DNA unwinding enzymes required to preserve genome integrity, thus preventing premature aging and cancer formation. The five human representatives of this family play non-redundant roles in the suppression of genome instability using a combination of enzymatic activities that specifically characterize each member of the family. These enzymes are in fact not only able to catalyze the transient opening of DN ... [truncated at 450 characters in length]|
|Author||Vindigni, Alessandro; Marino, Francesca; Gileadi, Opher;|
|Subject||DNA Repair DNA Replication DNA, Cruciform Genomic Instability Humans Protein Structure, Tertiary RecQ Helicases chemistry metabolism chemistry metabolism|
A prominent beta-hairpin structure in the winged-helix domain of RECQ1 is required for DNA unwinding and oligomer formation.
|Abstract||RecQ helicases have attracted considerable interest in recent years due to their role in the suppression of genome instability and human diseases. These atypical helicases exert their function by resolving a number of highly specific DNA structures. The crystal structure of a truncated catalytic core of the human RECQ1 helicase (RECQ1(49-616)) shows a prominent β-hairpin, with an aromatic residue (Y564) at the tip, located in the C-terminal winge ... [truncated at 450 characters in length]|
|Author||Lucic, Bojana; Zhang, Ying; King, Oliver; et al|
|Subject||DNA DNA, Cruciform Dimerization Humans Protein Multimerization Protein Structure, Secondary Protein Structure, Tertiary RecQ Helicases metabolism chemistry metabolism|