Dec 23, 2007 · Bailey, S., Eliason, W.K. & Steitz, T.A. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 318, 459–463 (2007). CAS Article Google Scholar
Get a quoteDuring DNA replication, bacterial helicase is recruited as a complex in association with loader proteins to unwind the parental duplex. Previous structural studies have reported saturated 6:6 helicase-loader complexes with different conformations.
Get a quoteSep 23, 2019 · As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized …
Get a quoteFeb 26, 2019 · Here, the helicase -- helicase loader complex is shown atop a set of cryogenic electron microscopy images used to visualize the structure. Credit: Jillian Chase and David Jeruzalmi
Get a quoteSep 19, 2013 · Structure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assembly September 2013 Nature Communications 4:2495
Get a quoteApr 25, 2003 · The Bacillus subtilis SPP1 phage-encoded protein G39P is a loader and inhibitor of the phage G40P replicative helicase involved in the initiation of DNA replication.We have carried out a full x-ray crystallographic and preliminary NMR analysis of G39P and functional studies of the protein, including assays for helicase binding by a number of truncated mutant forms, in an effort to improve our
Get a quoteBin Liu, William K. Eliason, Thomas A. Steitz Structure of a helicase-helicase loader complex reveals insights into mechanism of bacterial primosome assembly. Nature Communications 2013; 4:2495. doi: 10.1038/ncomms3495. Bin Liu, Jinzhong Lin, Thomas A. Steitz Structure of PolIIIα-τ c-DNA complex suggests an atomic model of the replisome.
Get a quoteApr 22, 2016 · In the 19 Å resolution EM map, the undistorted and unopened helicase ring holds a robust loader density above the C-terminal RecA-like domain. Meanwhile, the path of the central DNA binding channel appears to be obstructed by the reconstructed loader density, implying its potential role as a checkpoint conformation to prevent the loading of immature complex onto DNA.
Get a quote1 day ago · Comparison of overall structure of phiYY P4 and other helicases from SF1–6 reveals that the active center of NTP binding and hydrolysis of these enzymes are commonly located on the interface of two adjacent catalytic domains (RecA fold or AAA+ fold), helicases from SF1–2 have one catalytic interface, and the hexameric helicases from SF3–6
Get a quotePDB-101: Molecule of the Month: DNA Helicase
Get a quoteMar 19, 2015 · The ORC structure shows that the complex forms a lopsided, two-tiered ring with a cashew-shaped protuberance off of one edge (Fig. 1b, c and Supplementary Video 1). Orc1 through Orc5 comprise the ring body, which bears a prominent central channel, while a large domain insertion in Orc3 forms a bi-lobed, α-helical protuberance that engages a
Get a quoteFeb 24, 2017 · During the loading process, the helicase/helicase-loader complex probably still progresses through a 6:6 intermediate that encircles ssDNA (100, 101), and primase can bind to this dodecamer before helicase loader dissociation. However, precisely when certain factors bind to and release another, or how ATP turnover controls the helicase
Get a quoteApr 22, 2016 · Our data also reveals that the bound nucleotides and the consequently induced conformational changes in the helicase hexamer are essential for active association with loader proteins. These observations provide fundamental insights into the formation of the helicase-loader complex in bacteria that regulates the DNA replication process.
Get a quoteOct 14, 2011 · The RIG-I (ΔCARDs) dsRNA complex (A) Schematic representation of the RIG-I protein. The RIG-I (ΔCARDs) construct used for this study is boxed. (B) Overall structure of the RIG-I (ΔCARDs) dsRNA complex. Starting from the N-terminus: the helicase domain 1 (HEL1) is in green, the bridge between the two helicase domains grey, the helicase domain 2 (HEL2) blue, the insertion domain (HEL2i) cyan
Get a quoteMar 19, 2015 · The ORC structure shows that the complex forms a lopsided, two-tiered ring with a cashew-shaped protuberance off of one edge (Fig. 1b, c and Supplementary Video 1). Orc1 through Orc5 comprise the ring body, which bears a prominent central channel, while a large domain insertion in Orc3 forms a bi-lobed, α-helical protuberance that engages a
Get a quoteHexameric DnaB helicases are often loaded at DNA replication forks by interacting with the initiator protein DnaA and/or a helicase loader (DnaC in Escherichia coli). These loaders are not universally required, and DnaB from Helicobacter pylori was found to bypass DnaC when expressed in E. coli cells. The crystal structure of Helicobacter pylori DnaB C-terminal domain (HpDnaB-CTD) reveals a
Get a quoteMar 15, 2012 · Bin Liu, William K. Eliason, Thomas A. Steitz, Structure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assembly, Nature Communications, 10.1038/ncomms3495, 4, (2013).
Get a quoteApr 22, 2016 · This nearly undistorted structure describes a state after the recruitment of primase, which might consequently induce a conformational change in the preformed helicase-loader complex. Meanwhile, helicase-loader complexes with sub-stoichiometries (6:1 and 6:2) were also documented in B. subtilis species,,, but their structural detail is
Get a quote1 day ago · Comparison of overall structure of phiYY P4 and other helicases from SF1–6 reveals that the active center of NTP binding and hydrolysis of these enzymes are commonly located on the interface of two adjacent catalytic domains (RecA fold or AAA+ fold), helicases from SF1–2 have one catalytic interface, and the hexameric helicases from SF3–6
Get a quoteThe structure reveals that one N-terminal domain (NTD) of DnaC interacts with both the linker helix of a DnaB molecule and the C-terminal domain (CTD) of the adjacent DnaB molecule by forming a three α-helix bundle, which fixes the relative orientation of the two adjacent DnaB CTDs.
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