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Literature summary for 3.6.4.B8 extracted from

  • Alyami, E.M.; Rizzo, A.A.; Beuning, P.J.; Korzhnev, D.M.
    NMR resonance assignments for the N-terminal domain of the delta subunit of the E. coli gamma clamp loader complex (2017), Biomol. NMR Assign., 11, 169-173 .
    View publication on PubMed
Search for more literature for 3.6.4.B8

Cloned(Commentary)

Cloned (Comment) Organism
gene holA gene encodes the N-terminal domain (residues 1-140) of the Escherichia coli gamma clamp loader, recombinant His-tagged mini-delta is obtained by expression in Escherichia coli strain BL21(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of crystal structure of mini-delta taken from a structure of the mini-delta:beta-clamp I272A/L273A complex (PDB ID 1JQL) and of the X-ray crystal structures of the gamma clamp loader complex Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P28630 AND P28631 AND P06710 AND P28905 AND P28632 subunits delta, delta', gamma/tau, chi, and psi
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged mini-delta from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the His tag by thrombin, dialysis, and gel filtration Escherichia coli

Subunits

Subunits Comment Organism
More NMR resonance assignments for the N-terminal domain of the delta subunit of the gamma clamp loader complex. Nearly complete backbone and side-chain 1H, 13C and 15N NMR resonance assignments of mini-delta will facilitate NMR studies of the mechanisms of beta-clamp opening and its loading on DNA by the clamp loader Escherichia coli

Synonyms

Synonyms Comment Organism
clamp loader
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 Escherichia coli
clamp loader complex
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 Escherichia coli
gamma clamp loader
-
 Escherichia coli
gamma clamp loader complex
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the beta-clamp protein and the gamma clamp loader complex are essential components of bacterial DNA replication machinery. The beta-clamp is a ring-shaped homodimer that encircles DNA and increases the efficiency of replication by providing a binding platform for DNA polymerases and other replication-related proteins. The beta-clamp is loaded onto DNA by the five-subunit gamma clamp loader complex in a multi-step ATP-dependent process. The initial steps of this process involve the cooperative binding of the beta-clamp by the five subunits of ATP-bound clamp loader, which induces or traps an open conformation of the clamp. The delta subunit of the Escherichia coli clamp loader, or even its 140 residue N-terminal domain (called mini-delta), alone can shift conformational equilibrium of the beta-clamp towards the open state Escherichia coli