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

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, plays a central role in the organization and communication at the replication fork and present in initiation complex which is required for processive elongation.

Date:

2024-11-30