3LBF: Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli

Citation:
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 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.
PDB ID: 3LBFDownload
MMDB ID: 84660
PDB Deposition Date: 2010/1/8
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3LBF: monomeric; determined by author and by software (PISA)
Molecular Components in 3LBF
Label Count Molecule
Protein (1 molecule)
1
Protein-l-isoaspartate O-methyltransferase(Gene symbol: pcm)
Molecule annotation
Chemicals (4 molecules)
1
1
2
2
3
1
* Click molecule labels to explore molecular sequence information.

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