{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cho H"],"funding":["NIGMS NIH HHS"],"pagination":["8525-30"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC37469"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["98(15)"],"pubmed_abstract":["Protein phosphoaspartate bonds play a variety of roles. In response regulator proteins of two-component signal transduction systems, phosphorylation of an aspartate residue is coupled to a change from an inactive to an active conformation. In phosphatases and mutases of the haloacid dehalogenase (HAD) superfamily, phosphoaspartate serves as an intermediate in phosphotransfer reactions, and in P-type ATPases, also members of the HAD family, it serves in the conversion of chemical energy to ion gradients. In each case, lability of the phosphoaspartate linkage has hampered a detailed study of the phosphorylated form. For response regulators, this difficulty was recently overcome with a phosphate analog, BeF(3)(-), which yields persistent complexes with the active site aspartate of their recei"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase."],"pmcid":["PMC37469"],"funding_grant_id":["R01 GM062163","R01 GM038361","P50 GM62412","P50 GM062412","R37 GM038361","GM38361","GM62163"],"pubmed_authors":["Damo S","Cho H","Kim R","Kim SH","Wemmer D","Kustu S","Yan D","Wang W","Yokota H"],"additional_accession":[]},"is_claimable":false,"name":"BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase.","description":"Protein phosphoaspartate bonds play a variety of roles. In response regulator proteins of two-component signal transduction systems, phosphorylation of an aspartate residue is coupled to a change from an inactive to an active conformation. In phosphatases and mutases of the haloacid dehalogenase (HAD) superfamily, phosphoaspartate serves as an intermediate in phosphotransfer reactions, and in P-type ATPases, also members of the HAD family, it serves in the conversion of chemical energy to ion gradients. In each case, lability of the phosphoaspartate linkage has hampered a detailed study of the phosphorylated form. For response regulators, this difficulty was recently overcome with a phosphate analog, BeF(3)(-), which yields persistent complexes with the active site aspartate of their recei","dates":{"release":"2001-01-01T00:00:00Z","publication":"2001 Jul","modification":"2025-04-27T02:39:03.991Z","creation":"2019-03-26T22:30:38Z"},"accession":"S-EPMC37469","cross_references":{"pubmed":["11438683"],"doi":["10.1073/pnas.131213698"]}}