Phi29 polymerase structure
Webphi29 DNA Polymerase is the replicative polymerase from the Bacillus subtilis phage phi29 (Φ29) (1). This polymerase has exceptional strand displacement and processive synthesis properties (2). The polymerase has an inherent 3´→5' proofreading exonuclease activity (3). Web28. nov 2016 · The mutant phi29 DNA polymerase can perform WGA at elevated temperatures (40–42°C), generate two to five times more of DNA amplification products, and has significantly increased half-life at 30 and 40°C, both in the presence or the absence of DNA substrate. Introduction
Phi29 polymerase structure
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WebInitial structural studies provided insights into the intrinsic strand displacement, processivity, and protein priming activ-ities of phi29 DNAP. The structure of the apo phi29 DNAP exhibited two globular domains, an N-terminal exonuclease domain and a C-terminal polymerase domain. This structure contains three tunnels, one of which is formed ... Webstructure summary. Φ29 DNA polymerase is an enzyme from the bacteriophage Φ29. It is being increasingly used in molecular biology for multiple displacement DNA amplification procedures, and has a number of features that make …
Web22. mar 2006 · The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition The absolute requirement for primers in the initiation of DNA synthesis poses a problem for replicating the ends of linear chromosomes.
WebPhi29 DNA polymerase uses the OH group of a specific serine residue as a primer bypassing the need for a primase. During the extension stage the phi29 DNA polymerase continues to synthesize DNA in a standard DNA-primed fashion and the displaced single-stranded regions are covered by SSB. Web16. máj 2007 · Phi29 DNA polymerase complexed with primer-template DNA and incoming nucleotide substrates (ternary complex) PDB DOI: 10.2210/pdb2PYL/pdb NDB: PD1012 Classification: REPLICATION, TRANSFERASE/DNA Organism (s): Salasvirus phi29 Expression System: Escherichia coli Mutation (s): Yes Deposited: 2007-05-16 Released: …
Web29. jan 2024 · ϕ29 DNA polymerase is the only member of the protein-primed subgroup of DNA polymerases whose structure has been solved. It has a N-terminal domain (residues 1–189) with the 3′-5′ exonuclease...
Web28. jún 2024 · Disclosed herein is a specific B-family DNA polymerase variants that exhibit an improved incorporation of nucleotide analogues for synthesizing polynucleotides and sequencing the associated nucleic acid template. More particularly, the DNA sequencing-by-synthesis method can be efficiently performed by said B-family DNA polymerase variants … top 07060 car insuranceWeb21. sep 2004 · The DNA polymerase from phage phi29 is a B family polymerase that initiates replication using a protein as a primer, attaching the first nucleotide of the phage genome to the hydroxyl of a specific serine of the priming protein. The crystal structure of phi29 DNA polymerase determined at 2 ... Macromolecules Proteins 1 Nucleic Acids / … top 0720car insuranceWeb25. júl 2007 · To address this issue, we have determined the X-ray crystal structures of phi29 DNAP, a member of the protein-primed subgroup of the B-family of polymerases, complexed with primer-template DNA in the presence or absence of the incoming nucleoside triphosphate, the pre- and post-translocated states, respectively. pia headenWeb5. júl 2007 · The structure of the apo phi29 DNAP exhibited two globular domains, an N-terminal exonuclease domain and a C-terminal polymerase domain. This structure contains three tunnels, one of which is formed by the exonuclease domain and the palm and TP-interacting region 2 (TPR2) subdomains of the polymerase domain. top-07723Web30. sep 2024 · In a typical RCA, a circular template is isothermally amplified by Phi29 DNA polymerase at 30 °C, generating strands averaging 70 kb in length, which contain a large number of tandem repeats of the starting molecule. ... contained long self-complementary stretches that are respectively capable of forming a hairpin-loop structure by self ... top 07514 car insuranceWeb13. jún 2024 · Phi29 DNA polymerase, derived from Bacillus subtilis phage phi29, is widely used for DNA amplification through rolling-circle replication or multiple displacement amplification ( Dean et al., 2001; Dean et al., 2002) because of its high processivity ( Blanco et al., 1989 ), a strand displacement activity, high fidelity ( Esteban et al., 1993) and … top 07450 car insuranceWebphi29 DNA Polymerase is the replicative polymerase from the Bacillus subtilis phage phi29 (Φ29) (1). This polymerase has exceptional strand displacement and processive synthesis properties (2). The polymerase has an inherent 3´→5' proofreading exonuclease activity (3). Highlights Product Source top 07724 car insurance