Structural highlights
Function
[PIMT_ECOLI] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. This enzyme does not act on D-aspartyl residues.[HAMAP-Rule:MF_00090]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 A. 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.
Crystal structure of the protein L-isoaspartyl methyltransferase from Escherichia coli.,Fang P, Li X, Wang J, Xing L, Gao Y, Niu L, Teng M Cell Biochem Biophys. 2010 Dec;58(3):163-7. doi: 10.1007/s12013-010-9103-2. PMID:20857228[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2010 Dec;58(3):163-7. doi: 10.1007/s12013-010-9103-2. PMID:20857228 doi:http://dx.doi.org/10.1007/s12013-010-9103-2
