3OKG

Crystal structure of HsdS subunit from Thermoanaerobacter tengcongensis

3OKG の概要

• エントリーDOI: 10.2210/pdb3okg/pdb
• 分子名称: Restriction endonuclease S subunits, SULFATE ION (3 entities in total)
• 機能のキーワード: coiled-coil, type i methyltransferase, dna binding, dna binding protein
• 由来する生物種: Thermoanaerobacter tengcongensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 94483.66

構造登録者

Liang, D.,Gao, P.,Tang, Q.,An, X.,Yan, X. (登録日: 2010-08-24, 公開日: 2011-05-25, 最終更新日: 2024-03-20)

主引用文献

Gao, P.,Tang, Q.,An, X.,Yan, X.,Liang, D.
Structure of HsdS subunit from Thermoanaerobacter tengcongensis sheds lights on mechanism of dynamic opening and closing of type I methyltransferase
Plos One, 6:e17346-e17346, 2011

PubMed Abstract: Type I DNA methyltransferases contain one specificity subunit (HsdS) and two modification subunits (HsdM). The electron microscopy model of M.EcoKI-M₂S₁ methyltransferase shows a reasonable closed state of this clamp-like enzyme, but the structure of the open state is still unclear. The 1.95 Å crystal structure of the specificity subunit from Thermoanaerobacter tengcongensis (TTE-HsdS) shows an unreported open form inter-domain orientation of this subunit. Based on the crystal structure of TTE-HsdS and the closed state model of M.EcoKI-M₂S₁, we constructed a potential open state model of type I methyltransferase. Mutational studies indicated that two α-helices (aa30-59 and aa466-495) of the TTE-HsdM subunit are important inter-subunit interaction sites in the TTE-M₂S₁ complex. DNA binding assays also highlighted the importance of the C-terminal region of TTE-HsdM for DNA binding by the TTE-M₂S₁ complex. On the basis of structural analysis, biochemical experiments and previous studies, we propose a dynamic opening and closing mechanism for type I methyltransferase.

PubMed: 21399684
DOI: 10.1371/journal.pone.0017346

実験手法

X-RAY DIFFRACTION (1.95 Å)