3LBF

Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli

Summary for 3LBF

• Entry DOI: 10.2210/pdb3lbf/pdb
• Descriptor: Protein-L-isoaspartate O-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: modified rossman-type fold, methyltransferase, s-adenosyl-l-methionine, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A7A5
• Total number of polymer chains: 4
• Total formula weight: 96143.45

Authors

Fang, P.,Li, X.,Wang, J.,Niu, L.,Teng, M. (deposition date: 2010-01-08, release date: 2010-09-08, Last modification date: 2023-11-01)

Primary citation

Fang, P.,Li, X.,Wang, J.,Xing, L.,Gao, Y.,Niu, L.,Teng, M.
Crystal structure of the protein L-isoaspartyl methyltransferase from Escherichia coli
Cell Biochem.Biophys., 58:163-167, 2010

PubMed Abstract: Among the known covalent damages that can occur spontaneously to proteins, the formation of isoaspartyl linkages through deamidation of asparagines and isomerization of aspartates may be one of the most rapid forms under conditions of physiological pH and temperature. The protein L-isoaspartyl methyltransferase (PIMT) is thought to recognize L-isoaspartyl residues and repair this kind of damaged proteins. Curiously, there is a potential functional difference between bacterial and mammalian PIMTs. Herein, we present the crystal structure of Escherichia coli PIMT (EcPIMT) at a resolution of 1.8 Å. The enzyme we investigated was able to remain bound to its product S-adenosylhomocysteine (SAH) during crystallization. Analysis indicates that the high affinity of EcPIMT for SAH might lead to the lower activity of the enzyme.

PubMed: 20857228
DOI: 10.1007/s12013-010-9103-2

Experimental method

X-RAY DIFFRACTION (1.8 Å)