2HMY

BINARY COMPLEX OF HHAI METHYLTRANSFERASE WITH ADOMET FORMED IN THE PRESENCE OF A SHORT NONPSECIFIC DNA OLIGONUCLEOTIDE

2HMY の概要

• エントリーDOI: 10.2210/pdb2hmy/pdb
• 分子名称: PROTEIN (CYTOSINE-SPECIFIC METHYLTRANSFERASE HHAI), S-ADENOSYLMETHIONINE (3 entities in total)
• 機能のキーワード: transferase (methyltransferase)
• 由来する生物種: Haemophilus haemolyticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37440.64

構造登録者

O'Gara, M.,Zhang, X.,Roberts, R.J.,Cheng, X. (登録日: 1999-02-08, 公開日: 1999-03-19, 最終更新日: 2023-08-30)

主引用文献

O'Gara, M.,Zhang, X.,Roberts, R.J.,Cheng, X.
Structure of a binary complex of HhaI methyltransferase with S-adenosyl-L-methionine formed in the presence of a short non-specific DNA oligonucleotide.
J.Mol.Biol., 287:201-209, 1999

PubMed Abstract: We have determined a structure for a complex formed between HhaI methyltransferase (M.HhaI) and S-adenosyl-L-methionine (AdoMet) in the presence of a non-specific short oligonucleotide. M.HhaI binds to the non-specific short oligonucleotides in solution. Although no DNA is incorporated in the crystal, AdoMet binds in a primed orientation, identical with that observed in the ternary complex of the enzyme, cognate DNA, and AdoMet or S-adenosyl-L-homocysteine (AdoHcy). This orientation differs from the previously observed unprimed orientation in the M.HhaI-AdoMet binary complex, where the S+-CH3 unit of AdoMet is protected by a favorable cation-pi interaction with Trp41. The structure suggests that the presence of DNA can guide AdoMet into the primed orientation. These results shed new light on the proposed ordered mechanism of binding and explains the stable association between AdoMet and M.HhaI.

PubMed: 10080885
DOI: 10.1006/jmbi.1999.2608

実験手法

X-RAY DIFFRACTION (2.61 Å)