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Helicases are a class of enzymes that are vital to all organisms. Their main function is to unpack an organism's genetic material. Helicases are motor proteins that move directionally along a nucleic double helix, separating the two hybridized nucleic acid strands (hence helic-+ -ase), via the energy gained from ATP hydrolysis. There are many ...
DEAD box proteins were first brought to attention in the late 1980s in a study that looked at a group of NTP binding sites that were similar in sequence to the eIF4A RNA helicase sequence. [4] The results of this study showed that these proteins (p68, SrmB, MSS116, vasa, PL10, mammalian eIF4A, yeast eIF4A) involved in RNA metabolism had several ...
Pages in category "Helicases" The following 27 pages are in this category, out of 27 total. This list may not reflect recent changes. B. Bloom syndrome protein;
104721 Ensembl ENSG00000079785 ENSMUSG00000037149 UniProt Q92499 Q91VR5 RefSeq (mRNA) NM_004939 NM_134040 RefSeq (protein) NP_004930 NP_598801 Location (UCSC) Chr 2: 15.59 – 15.63 Mb Chr 12: 13.27 – 13.3 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse ATP-dependent RNA helicase DDX1 is an enzyme that in humans is encoded by the DDX1 gene. Function DEAD box proteins, characterized ...
T7 DNA helicase (gp4) is a hexameric motor protein encoded by T7 phages that uses energy from dTTP hydrolysis to process unidirectionally along single stranded DNA, separating the two strands as it progresses. It is also a primase, making short stretches of RNA that initiates DNA synthesis. [2]
A helicase–primase complex (also helicase-primase, Hel/Prim, H-P or H/P) is a complex of enzymes including DNA helicase and DNA primase. A helicase-primase associated factor protein may also be present. [1] The complex is used by herpesviruses, in which it is responsible for lytic DNA virus replication.
The structure of the helicase has been solved at high resolution and indicates "inchworming" as the mechanism of translocation on single-stranded DNA. A Mexican-wave model has been proposed based on the changes in conformation of the helicase observed in the product versus substrate complex.
Structurally, DHX36 is a 1008 amino acid-long modular protein that has been crystallized in a complex with a DNA G-quadruplex. [6] It consists of a ~440-amino acid helicase core comprising all signature motifs of the DEAH/RHA family of helicases with N- and C-terminal flanking regions of ~180 and ~380 amino acids, respectively.