1I1N

HUMAN PROTEIN L-ISOASPARTATE O-METHYLTRANSFERASE WITH S-ADENOSYL HOMOCYSTEINE

1I1N の概要

• エントリーDOI: 10.2210/pdb1i1n/pdb
• 関連するPDBエントリー: 1DL5
• 分子名称: PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: methyltransferase, s-adenosyl homocysteine, protein repair, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P22061
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24921.62

構造登録者

Smith, C.D.,Chattopadhyay, D.,Carson, M.,Friedman, A.M.,Skinner, M.M. (登録日: 2001-02-02, 公開日: 2002-03-13, 最終更新日: 2023-08-09)

主引用文献

Smith, C.D.,Carson, M.,Friedman, A.M.,Skinner, M.M.,Delucas, L.,Chantalat, L.,Weise, L.,Shirasawa, T.,Chattopadhyay, D.
Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-A resolution and modeling of an isoaspartyl-containing peptide at the active site.
Protein Sci., 11:625-635, 2002

PubMed Abstract: Spontaneous formation of isoaspartyl residues (isoAsp) disrupts the structure and function of many normal proteins. Protein isoaspartyl methyltransferase (PIMT) reverts many isoAsp residues to aspartate as a protein repair process. We have determined the crystal structure of human protein isoaspartyl methyltransferase (HPIMT) complexed with adenosyl homocysteine (AdoHcy) to 1.6-A resolution. The core structure has a nucleotide binding domain motif, which is structurally homologous with the N-terminal domain of the bacterial Thermotoga maritima PIMT. Highly conserved residues in PIMTs among different phyla are placed at positions critical to AdoHcy binding and orienting the isoAsp residue substrate for methylation. The AdoHcy is completely enclosed within the HPIMT and a conformational change must occur to allow exchange with adenosyl methionine (AdoMet). An ordered sequential enzyme mechanism is supported because C-terminal residues involved with AdoHcy binding also form the isoAsp peptide binding site, and a change of conformation to allow AdoHcy to escape would preclude peptide binding. Modeling experiments indicated isoAsp groups observed in some known protein crystal structures could bind to the HPIMT active site.

PubMed: 11847284
DOI: 10.1110/ps.37802

実験手法

X-RAY DIFFRACTION (1.5 Å)