- PDB-2atq: RB69 single-stranded DNA binding protein-DNA polymerase fusion -
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Basic information
Entry
Database: PDB / ID: 2atq
Title
RB69 single-stranded DNA binding protein-DNA polymerase fusion
Components
DNA polymerase
gp32
Keywords
TRANSFERASE/DNA BINDING PROTEIN / DNA polymerase / palm domain / fingers domain / thumb domain / single-stranded DNA binding protein / OB-fold / TRANSFERASE-DNA BINDING PROTEIN COMPLEX
Function / homology
Function and homology information
bidirectional double-stranded viral DNA replication / Hydrolases; Acting on ester bonds; Exodeoxyribonucleases producing 5'-phosphomonoesters / nucleotide-excision repair, DNA gap filling / DNA replication proofreading / 3'-5'-DNA exonuclease activity / SOS response / 3'-5' exonuclease activity / base-excision repair, gap-filling / single-stranded DNA binding / DNA recombination ...bidirectional double-stranded viral DNA replication / Hydrolases; Acting on ester bonds; Exodeoxyribonucleases producing 5'-phosphomonoesters / nucleotide-excision repair, DNA gap filling / DNA replication proofreading / 3'-5'-DNA exonuclease activity / SOS response / 3'-5' exonuclease activity / base-excision repair, gap-filling / single-stranded DNA binding / DNA recombination / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / DNA repair / nucleotide binding / DNA binding / metal ion binding Similarity search - Function
Replication Fork Single-Stranded DNA Binding Protein / Replication Fork Single-Stranded Dna Binding Protein / Bacteriophage T4, Gp32, single-stranded DNA-binding domain / Bacteriophage T4, Gp32, single-stranded DNA-binding superfamily / Bacteriophage T4, Gp32, single-stranded DNA-binding / gp32 DNA binding protein like / Monooxygenase - #300 / DNA-directed DNA polymerase T4 type / DNA Polymerase; Chain A, domain 1 / DNA Polymerase, chain B, domain 1 ...Replication Fork Single-Stranded DNA Binding Protein / Replication Fork Single-Stranded Dna Binding Protein / Bacteriophage T4, Gp32, single-stranded DNA-binding domain / Bacteriophage T4, Gp32, single-stranded DNA-binding superfamily / Bacteriophage T4, Gp32, single-stranded DNA-binding / gp32 DNA binding protein like / Monooxygenase - #300 / DNA-directed DNA polymerase T4 type / DNA Polymerase; Chain A, domain 1 / DNA Polymerase, chain B, domain 1 / B family DNA polymerase, finger domain / Palm domain of DNA polymerase / B family DNA polymerase, palm domain / Monooxygenase / DNA polymerase family B signature. / DNA-directed DNA polymerase, family B, conserved site / DNA polymerase family B / DNA polymerase family B, exonuclease domain / DNA-directed DNA polymerase, family B, exonuclease domain / DNA-directed DNA polymerase, family B, multifunctional domain / DNA polymerase, palm domain superfamily / DNA polymerase type-B family / DNA-directed DNA polymerase, family B / Ribonuclease H-like superfamily/Ribonuclease H / Helix Hairpins / Nucleotidyltransferase; domain 5 / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Nucleic acid-binding, OB-fold / DNA/RNA polymerase superfamily / Alpha-Beta Complex / Up-down Bundle / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / DNA-directed DNA polymerase / Single-stranded DNA-binding protein Similarity search - Component
Biological species
Enterobacteria phage RB69 (virus)
Method
X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3.2 Å
Journal: Proteins / Year: 2006 Title: Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity. Authors: Sun, S. / Geng, L. / Shamoo, Y.
SEQUENCE THE C-TERMINUS OF RB69 SINGLE-STRANDED DNA BINDING PROTEIN CORE DOMAIN IS FUSED TO THE N- ...SEQUENCE THE C-TERMINUS OF RB69 SINGLE-STRANDED DNA BINDING PROTEIN CORE DOMAIN IS FUSED TO THE N-TERMINUS OF DNA POLYMERASE THROUGH A LINKER CONSISTING OF GTGSGT. THE LINKER WAS NOT OBSERVED IN THE DENSITY.
Mass: 104655.141 Da / Num. of mol.: 1 / Mutation: D222A, D327A Source method: isolated from a genetically manipulated source Details: C-terminus is fused to a linker not seen in the density Source: (gene. exp.) Enterobacteria phage RB69 (virus) / Genus: T4-like viruses / Gene: 43 / Plasmid: pET101 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q38087, DNA-directed DNA polymerase
#2: Protein
gp32
Mass: 26228.523 Da / Num. of mol.: 1 / Fragment: RB69 single-stranded DNA binding protein Source method: isolated from a genetically manipulated source Details: N-terminus is fused to a linker not seen in the density Source: (gene. exp.) Enterobacteria phage RB69 (virus) / Genus: T4-like viruses / Gene: gp32 / Plasmid: pET101 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q7Y265
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