{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11(3)"],"submitter":["Smith CD"],"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 chan"],"journal":["Protein science : a publication of the Protein Society"],"pagination":["625-35"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2373461"],"repository":["biostudies-literature"],"pubmed_title":["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."],"pmcid":["PMC2373461"],"pubmed_authors":["Friedman AM","Chantalat L","Shirasawa T","Smith CD","Carson M","Skinner MM","Chattopadhyay D","Delucas L","Weise L"],"additional_accession":[]},"is_claimable":false,"name":"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.","description":"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 chan","dates":{"release":"2002-01-01T00:00:00Z","publication":"2002 Mar","modification":"2025-04-27T00:21:49.974Z","creation":"2019-03-27T02:45:00Z"},"accession":"S-EPMC2373461","cross_references":{"pubmed":["11847284"],"doi":["10.1110/ps.37802"]}}