Protein Family Models

This entry represents the C-terminal domain of the delta subunit from the clamp-loader complex of Bacillus subtilis and other Gram-positive bacteria, which is structurally similar to that of the DNApol3 delta subunit from E.coli [1-3]. This domain interacts with other subunits in the complex (tau and delta') and the nature of these interactions appear to be hydrophilic in contrast with the one observed in Gram-negative bacteria [3]. Paper describing PDB structure 1jqj. [1]. 11525728. Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III. Jeruzalmi D, Yurieva O, Zhao Y, Young M, Stewart J, Hingorani M, O'Donnell M, Kuriyan J;. Cell. 2001;106:417-428. Paper describing PDB structure 3glf. [2]. 19450514. The mechanism of ATP-dependent primer-template recognition by a clamp loader complex. Simonetta KR, Kazmirski SL, Goedken ER, Cantor AJ, Kelch BA, McNally R, Seyedin SN, Makino DL, O'Donnell M, Kuriyan J;. Cell. 2009;137:659-671. Paper describing PDB structure 3zh9. [3]. 23525462. Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase. Afonso JP, Chintakayala K, Suwannachart C, Sedelnikova S, Giles K, Hoyes JB, Soultanas P, Rafferty JB, Oldham NJ;. Nucleic Acids Res. 2013;41:5115-5126. (from Pfam)

Date:

2024-10-16

This domain lies at the C-terminus of the delta subunit of the DNA polymerase III clamp loader gamma complex. Within the complex the several C-terminal domains, of gamma, delta and delta' form a helical scaffold, on which the rest of he subunits are hung. The gamma complex, an AAA+ ATPase, is the bacterial homologue of the eukaryotic replication factor C that loads the sliding clamp (beta, homologous to PCNA) onto DNA. [1]. 11525729. Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Jeruzalmi D, O'Donnell M, Kuriyan J;. Cell. 2001;106:429-441. (from Pfam)

Date:

2024-10-16

DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalysed reaction [1]. The delta subunit is also known as HolA. This entry represents the ATPase domain [1,2] [1]. 11432857. The delta and delta ' subunits of the DNA polymerase III holoenzyme are essential for initiation complex formation and processive elongation. Song MS, Pham PT, Olson M, Carter JR, Franden MA, Schaaper RM, McHenry CS;. J Biol Chem 2001;276:35165-35175. [2]. 19450514. The mechanism of ATP-dependent primer-template recognition by a clamp loader complex. Simonetta KR, Kazmirski SL, Goedken ER, Cantor AJ, Kelch BA, McNally R, Seyedin SN, Makino DL, O'Donnell M, Kuriyan J;. Cell. 2009;137:659-671. (from Pfam)

Date:

2024-10-16

DNA polymerase III delta (holA) and delta-prime (holB) subunits are distinct proteins encoded by separate genes. The delta, delta-prime, gamma, chi and psi subunits form the gamma complex subassembly of DNA polymerase III holoenzyme, which couples ATP to assemble the ring-shaped beta subunit around DNA forming a DNA sliding clamp.

Gene:

holA

Date:

2024-05-14

DNA polymerase III subunit delta interacts with the delta' and gamma subunits and is part of the clamp-loading complex, which assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork

Date:

2023-02-23