Cloned (Comment) | Organism |
---|---|
genes dnaX, and holA-D | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Escherichia coli | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P28630 AND P28631 AND P06710 AND P28905 AND P28632 | subunits delta, delta', gamma/tau, chi, and psi | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Escherichia coli | ADP + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
heptamer | the Escherichia coli clamp loader complex CLC comprises seven subunits: delta, tau_n, gamma(3-n), delta', psi, and chi. The delta and delta' subunits (encoded by holA and holB) together with three copies of gamma and/or tau (encoded by dnaX) form a heteropentamer. The chi and psi subunits (encoded by holC and holD) are not required for clamp-loading activity, but serve to bridge the CLC with single-stranded DNA (ssDNA)-binding protein (SSB). The gamma subunit is a truncated (residues 1-431) form of tau (residues 1-643) resulting from a programmed frameshift during translation of dnaX mRNA. Enzyme pentameric and heptameric complex structures with bound DNA or SSB and without, overview. The pentameric deltagamma3delta' complex in the apo, ADP-, or ATP-gammaS-bound states are nearly identical | Escherichia coli |
More | clamp loader complex organization of tau domains, the truncated version gamma comprises domains I-III, overview | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
ATP-dependent clamp loader complex | - |
Escherichia coli |
clamp loader complex | - |
Escherichia coli |
CLC | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
additional information | structure of Escherichia coli clamp loader complex CLC in complex with primed template DNA (PDB ID 3GLI). The chi and psi subunits serve to link the clamp loader complex and ssDNA binding protein SSB, with chi binding to SSB. Through its interaction with the CLC and SSB, the chi-psi complex plays an important role in the processivity of Okazaki fragment synthesis. Folds of chi and psi are similar to mononucleotide and dinucleotide binding proteins, respectively | Escherichia coli |
physiological function | sliding clamps are actively loaded onto primed template DNA by ATP-dependent clamp loader complexes. The complex of chi and psi enzyme complex subunits plays an important role in the processivity of Okazaki fragment synthesis | Escherichia coli |