1G60

Crystal Structure of Methyltransferase MboIIa (Moraxella bovis)

1G60 の概要

• エントリーDOI: 10.2210/pdb1g60/pdb
• 分子名称: Adenine-specific Methyltransferase MboIIA, SODIUM ION, S-ADENOSYLMETHIONINE, ... (4 entities in total)
• 機能のキーワード: structural genomics, moraxella bovis, dna methylation, s-adenosylmethionine, psi, protein structure initiative, midwest center for structural genomics, mcsg, transferase
• 由来する生物種: Moraxella bovis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61227.64

構造登録者

Osipiuk, J.,Walsh, M.A.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2000-11-02, 公開日: 2002-05-01, 最終更新日: 2024-02-07)

主引用文献

Osipiuk, J.,Walsh, M.A.,Joachimiak, A.
Crystal structure of MboIIA methyltransferase.
Nucleic Acids Res., 31:5440-5448, 2003

PubMed Abstract: DNA methyltransferases (MTases) are sequence-specific enzymes which transfer a methyl group from S-adenosyl-L-methionine (AdoMet) to the amino group of either cytosine or adenine within a recognized DNA sequence. Methylation of a base in a specific DNA sequence protects DNA from nucleolytic cleavage by restriction enzymes recognizing the same DNA sequence. We have determined at 1.74 A resolution the crystal structure of a beta-class DNA MTase MboIIA (M.MboIIA) from the bacterium Moraxella bovis, the smallest DNA MTase determined to date. M.MboIIA methylates the 3' adenine of the pentanucleotide sequence 5'-GAAGA-3'. The protein crystallizes with two molecules in the asymmetric unit which we propose to resemble the dimer when M.MboIIA is not bound to DNA. The overall structure of the enzyme closely resembles that of M.RsrI. However, the cofactor-binding pocket in M.MboIIA forms a closed structure which is in contrast to the open-form structures of other known MTases.

PubMed: 12954781
DOI: 10.1093/nar/gkg713

実験手法

X-RAY DIFFRACTION (1.74 Å)