4BEC

MUTANT (K220A) OF THE HSDR SUBUNIT OF THE ECOR124I RESTRICTION ENZYME IN COMPLEX WITH ATP

4BEC の概要

• エントリーDOI: 10.2210/pdb4bec/pdb
• 関連するPDBエントリー: 4BE7 4BEB
• 分子名称: TYPE I RESTRICTION ENZYME HSDR, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: hydrolase, dna modification
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 241504.53

構造登録者

Csefalvay, E.,Lapkouski, M.,Guzanova, A.,Csefalvay, L.,Baikova, T.,Shevelev, I.,Janscak, P.,Smatanova, I.K.,Panjikar, S.,Carey, J.,Weiserova, M.,Ettrich, R. (登録日: 2013-03-07, 公開日: 2014-03-26, 最終更新日: 2023-12-20)

主引用文献

Csefalvay, E.,Lapkouski, M.,Guzanova, A.,Csefalvay, L.,Baikova, T.,Shevelev, I.,Bialevich, V.,Shamayeva, K.,Janscak, P.,Kuta Smatanova, I.,Panjikar, S.,Carey, J.,Weiserova, M.,Ettrich, R.
Functional Coupling of Duplex Translocation to DNA Cleavage in a Type I Restriction Enzyme.
Plos One, 10:28700-, 2015

PubMed Abstract: Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA cleavage and ATP-dependent DNA translocation activities located on motor subunit HsdR. Functional coupling of DNA cleavage and translocation is a hallmark of the Type I restriction systems that is consistent with their proposed role in horizontal gene transfer. DNA cleavage occurs at nonspecific sites distant from the cognate recognition sequence, apparently triggered by stalled translocation. The X-ray crystal structure of the complete HsdR subunit from E. coli plasmid R124 suggested that the triggering mechanism involves interdomain contacts mediated by ATP. In the present work, in vivo and in vitro activity assays and crystal structures of three mutants of EcoR124I HsdR designed to probe this mechanism are reported. The results indicate that interdomain engagement via ATP is indeed responsible for signal transmission between the endonuclease and helicase domains of the motor subunit. A previously identified sequence motif that is shared by the RecB nucleases and some Type I endonucleases is implicated in signaling.

PubMed: 26039067
DOI: 10.1371/JOURNAL.PONE.0128700

実験手法

X-RAY DIFFRACTION (2.84 Å)