Structural Analysis of Bacillus subtilis SPP1 Phage
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 …
Get a quote
EM structure of a helicase-loader complex depicting a 6: 2
During 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 quote
EM structure of a helicase-loader complex depicting a 6: 2
During 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 quote
PDB-101: Molecule of the Month: DNA Helicase
A second protein, a helicase loader, assists the initiator and chaperones the replicative DNA helicase onto the single strand. The structure shown here (PDB entry 4m4w ) includes DNA helicase (blue), a helicase loader (magenta) and a small domain from primase (green), the enzyme that will build the short RNA primer that gets replication started. This low-resolution …
Get a quote
Cryo-EM Structure of an Extended SARS-CoV-2 Replication
Transcription of SARS-CoV-2 mRNA requires sequential reactions facilitated by the replication and transcription complex (RTC). Here, we present a structural snapshot of SARS-CoV-2 RTC as it transitions toward cap structure synthesis. We determine the atomic cryo-EM structure of an extended RTC assem …
Get a quote
EM structure of a helicase-loader complex depicting a 6:2
Apr 22, 2016 · Recently, a cross-species crystal structure of a Gram-positive BstDnaG HBD-BstDnaB-BsuDnaI (primase (Helicase Binding Domain)-helicase-loader) complex was determined with a 3:6:6 stoichiometry . This nearly undistorted structure describes a state after the recruitment of primase, which might consequently induce a conformational change in the …
Get a quote
The clamp-loader-helicase interaction in Bacillus. Atomic
Feb 13, 2004 · The tau subunit of the clamp-loader mediates the interaction with DnaB. We have recently characterised this interaction in the Bacillus system and established a tau(5)-DnaB(6) stoichiometry. Here, we have obtained atomic force microscopy images of the tau-DnaB complex that reveal the first structural insight into its architecture.
Get a quote
DNA binding activity of Helicobacter pylori DnaB helicase
Annu Rev Biochem 69, 651–697. Mapping protein–protein interactions within a stable 5 Bailey S, Eliason WK & Steitz TA (2007) The crystal complex of DnaG primase and DnaB helicase structure of the Thermus aquaticus DnaB helicase from Bacillus …
Get a quote
RCSB PDB - 6KZA: Crystal structure of the complex of the
Sep 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 …
Get a quote
EM structure of a helicase-loader complex depicting a 6:2
Apr 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 quote
Structure of the PolIIIα-τc-DNA complex suggests an atomic
The C-terminal domain (CTD) of the τ subunit of the clamp loader (τc) binds to both the DnaB helicase and the DNA polymerase III α subunit (PolIIIα), and determines their relative positions and orientations on the leading and lagging strands. Here, we present a 3.2 Å resolution structure of Thermus aquaticus PolIIIα in complex with τc
Get a quote
Physical Basis for the Loading of a Bacterial Replicative
Arias-Palomo et al. present the cryo-EM structures of a replicative bacterial helicase-loader complex (E. coli DnaBC) in pre- and post-loading states, revealing how the loader breaks the helicase ring to deposit it at the origin of replication and how ssDNA engagement closes and activates the helicase.
Get a quote
RCSB PDB - 6DUQ: Structure of a Rho-NusG KOW domain complex
Jun 21, 2018 · Here, we demonstrate that NusG activates Rho by assisting helicase isomerization from an open-ring, RNA-loading state to a closed-ring, catalytically active translocase. A crystal structure of closed-ring Rho in complex with NusG reveals the physical basis for this activation and further explains how Rho is excluded from translationally
Get a quote
Untangling the roles of RNA helicases in antiviral innate
Dec 09, 2021 · Cryo-electron microscopy revealed that hsDicer adopts an L-shaped structure where the helicase domain is located in the shorter arm [22,35,36] . The 3 subdomains of the DExD/H-box helicase form a C-shaped structure in which HEL1 is at the junction between the 2 parts of the "L" and interacts with DUF283 and RNaseIIIb.
Get a quote
Mechanisms for initiating cellular DNA replication
Feb 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 quote
Untangling the roles of RNA helicases in antiviral innate
Dec 09, 2021 · Cryo-electron microscopy revealed that hsDicer adopts an L-shaped structure where the helicase domain is located in the shorter arm [22,35,36] . The 3 subdomains of the DExD/H-box helicase form a C-shaped structure in which HEL1 is at the junction between the 2 parts of the "L" and interacts with DUF283 and RNaseIIIb.
Get a quote(PDF) Structure of a helicase–helicase loader complex
Sep 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 quote
DNA binding activity of Helicobacter pylori DnaB helicase
Annu Rev Biochem 69, 651–697. Mapping protein–protein interactions within a stable 5 Bailey S, Eliason WK & Steitz TA (2007) The crystal complex of DnaG primase and DnaB helicase structure of the Thermus aquaticus DnaB helicase from Bacillus …
Get a quote
Crystal structure of the complex of the interaction
The 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.
Get a quote
RCSB PDB - 6DUQ: Structure of a Rho-NusG KOW domain complex
Jun 21, 2018 · Here, we demonstrate that NusG activates Rho by assisting helicase isomerization from an open-ring, RNA-loading state to a closed-ring, catalytically active translocase. A crystal structure of closed-ring Rho in complex with NusG reveals the physical basis for this activation and further explains how Rho is excluded from translationally
Get a quote
