1DCT

DNA (CYTOSINE-5) METHYLASE FROM HAEIII COVALENTLY BOUND TO DNA

1DCT の概要

• エントリーDOI: 10.2210/pdb1dct/pdb
• 分子名称: DNA (5'-D(*AP*CP*CP*AP*GP*CP*AP*GP*GP*(C49)P*CP*AP*CP*CP*AP*GP*TP*G)-3'), DNA (5'-D(*TP*CP*AP*CP*TP*GP*GP*TP*GP*GP*(C5M)P*CP*TP*GP*CP*TP*GP*G)-3'), PROTEIN (MODIFICATION METHYLASE HAEIII), ... (4 entities in total)
• 機能のキーワード: enzyme, cytosine methylase, transferase-dna complex, transferase/dna
• 由来する生物種: Haemophilus influenzae biotype aegyptius
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 96493.76

構造登録者

Reinisch, K.M.,Chen, L.,Verdine, G.L.,Lipscomb, W.N. (登録日: 1995-05-17, 公開日: 1995-09-15, 最終更新日: 2024-10-09)

主引用文献

Reinisch, K.M.,Chen, L.,Verdine, G.L.,Lipscomb, W.N.
The crystal structure of HaeIII methyltransferase convalently complexed to DNA: an extrahelical cytosine and rearranged base pairing.
Cell(Cambridge,Mass.), 82:143-153, 1995

PubMed Abstract: Many organisms expand the information content of their genome through enzymatic methylation of cytosine residues. Here we report the 2.8 A crystal structure of a bacterial DNA (cytosine-5)-methyltransferase (DCMtase), M. HaeIII, bound covalently to DNA. In this complex, the substrate cytosine is extruded from the DNA helix and inserted into the active site of the enzyme, as has been observed for another DCMtase, M. HhaI. The DNA is bound in a cleft between the two domains of the protein and is distorted from the characteristic B-form conformation at its recognition sequence. A comparison of structures shows a variation in the mode of DNA recognition: M. HaeIII differs from M. HhaI in that the remaining bases in its recognition sequence undergo an extensive rearrangement in their pairing. In this process, the bases are unstacked, and a gap 8 A long opens in the DNA.

PubMed: 7606780
DOI: 10.1016/0092-8674(95)90060-8

実験手法

X-RAY DIFFRACTION (2.8 Å)