1DL5

PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE

Summary for 1DL5

• Entry DOI: 10.2210/pdb1dl5/pdb
• Descriptor: PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE, CADMIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: methyltransferase, isoaspartyl residues, protein repair, deamidation, post-translational modification, transferase
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm (By similarity): Q56308
• Total number of polymer chains: 2
• Total formula weight: 75016.72

Authors

Skinner, M.M.,Puvathingal, J.M.,Walter, R.L.,Friedman, A.M. (deposition date: 1999-12-08, release date: 2000-12-08, Last modification date: 2024-11-20)

Primary citation

Skinner, M.M.,Puvathingal, J.M.,Walter, R.L.,Friedman, A.M.
Crystal structure of protein isoaspartyl methyltransferase: a catalyst for protein repair.
Structure Fold.Des., 8:1189-1201, 2000

PubMed Abstract: Formation of isoaspartyl residues is one of several processes that damage proteins as they age. Protein L-isoaspartate (D-aspartate) O-methyltransferase (PIMT) is a conserved and nearly ubiquitous enzyme that catalyzes the repair of proteins damaged by isoaspartyl formation.

PubMed: 11080641
DOI: 10.1016/S0969-2126(00)00522-0

Experimental method

X-RAY DIFFRACTION (1.8 Å)