3JA9

Structure of native human PCNA

3JA9 の概要

• エントリーDOI: 10.2210/pdb3ja9/pdb
• EMDBエントリー: 6339
• 分子名称: Proliferating cell nuclear antigen (2 entities in total)
• 機能のキーワード: dna, replication, processivity, oncogene, dna-binding systemic lupus erythematosus, dna binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 86387.26

構造登録者

Lau, W.C.Y.,Li, Y.,Zhang, Q.,Huen, M.S.Y. (登録日: 2015-05-19, 公開日: 2015-12-09, 最終更新日: 2024-10-16)

主引用文献

Lau, W.C.,Li, Y.,Zhang, Q.,Huen, M.S.
Molecular architecture of the Ub-PCNA/Pol eta complex bound to DNA
Sci Rep, 5:15759-15759, 2015

PubMed Abstract: Translesion synthesis (TLS) is the mechanism by which DNA polymerases replicate through unrepaired DNA lesions. TLS is activated by monoubiquitination of the homotrimeric proliferating cell nuclear antigen (PCNA) at lysine-164, followed by the switch from replicative to specialized polymerases at DNA damage sites. Pol η belongs to the Y-Family of specialized polymerases that can efficiently bypass UV-induced lesions. Like other members of the Y-Family polymerases, its recruitment to the damaged sites is mediated by the interaction with monoubiquitinated PCNA (Ub-PCNA) via its ubiquitin-binding domain and non-canonical PCNA-interacting motif in the C-terminal region. The structural determinants underlying the direct recognition of Ub-PCNA by Pol η, or Y-Family polymerases in general, remain largely unknown. Here we report a structure of the Ub-PCNA/Pol η complex bound to DNA determined by single-particle electron microscopy (EM). The overall obtained structure resembles that of the editing PCNA/PolB complex. Analysis of the map revealed the conformation of ubiquitin that binds the C-terminal domain of Pol η. Our present study suggests that the Ub-PCNA/Pol η interaction requires the formation of a structured binding interface, which is dictated by the inherent flexibility of Ub-PCNA.

PubMed: 26503230
DOI: 10.1038/srep15759

実験手法

ELECTRON MICROSCOPY (22 Å)