2V6E

protelomerase TelK complexed with substrate DNA

2V6E の概要

• エントリーDOI: 10.2210/pdb2v6e/pdb
• 分子名称: PROTELEMORASE, TELRL, VANADATE ION, ... (4 entities in total)
• 機能のキーワード: hairpin telomere, hydrolase, resolvase, protelomerase, dna distortion
• 由来する生物種: KLEBSIELLA PHAGE PHIKO2; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 155713.74

構造登録者

Aihara, H.,Huang, W.M.,Ellenberger, T. (登録日: 2007-07-17, 公開日: 2007-10-02, 最終更新日: 2024-05-08)

主引用文献

Aihara, H.,Huang, W.M.,Ellenberger, T.
An Interlocked Dimer of the Protelomerase Telk Distorts DNA Structure for the Formation of Hairpin Telomeres
Mol.Cell, 27:901-, 2007

PubMed Abstract: The termini of linear chromosomes are protected by specialized DNA structures known as telomeres that also facilitate the complete replication of DNA ends. The simplest type of telomere is a covalently closed DNA hairpin structure found in linear chromosomes of prokaryotes and viruses. Bidirectional replication of a chromosome with hairpin telomeres produces a catenated circular dimer that is subsequently resolved into unit-length chromosomes by a dedicated DNA cleavage-rejoining enzyme known as a hairpin telomere resolvase (protelomerase). Here we report a crystal structure of the protelomerase TelK from Klebsiella oxytoca phage varphiKO2, in complex with the palindromic target DNA. The structure shows the TelK dimer destabilizes base pairing interactions to promote the refolding of cleaved DNA ends into two hairpin ends. We propose that the hairpinning reaction is made effectively irreversible by a unique protein-induced distortion of the DNA substrate that prevents religation of the cleaved DNA substrate.

PubMed: 17889664
DOI: 10.1016/J.MOLCEL.2007.07.026

実験手法

X-RAY DIFFRACTION (3.2 Å)