4K74

The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.

4K74 の概要

• エントリーDOI: 10.2210/pdb4k74/pdb
• 分子名称: DNA polymerase III subunit beta, UmuC peptide (3 entities in total)
• 機能のキーワード: dna replication clamp processivity factor, dna replication/repair, dna binding protein-transferase complex, dna binding protein/transferase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q1R4N6
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 85563.65

構造登録者

Patoli, A.A.,Winter, J.A.,Bunting, K.A. (登録日: 2013-04-16, 公開日: 2013-07-17, 最終更新日: 2023-09-20)

主引用文献

Patoli, A.A.,Winter, J.A.,Bunting, K.A.
The UmuC subunit of the E. coli DNA polymerase V shows a unique interaction with the beta-clamp processivity factor.
Bmc Struct.Biol., 13:12-12, 2013

PubMed Abstract: Strict regulation of replisome components is essential to ensure the accurate transmission of the genome to the next generation. The sliding clamp processivity factors play a central role in this regulation, interacting with both DNA polymerases and multiple DNA processing and repair proteins. Clamp binding partners share a common peptide binding motif, the nature of which is essentially conserved from phage through to humans. Given the degree of conservation of these motifs, much research effort has focussed on understanding how the temporal and spatial regulation of multiple clamp binding partners is managed. The bacterial sliding clamps have come under scrutiny as potential targets for rational drug design and comprehensive understanding of the structural basis of their interactions is crucial for success.

PubMed: 23822808
DOI: 10.1186/1472-6807-13-12

実験手法

X-RAY DIFFRACTION (2.5 Å)