From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1r18.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1r18.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1r18| PDB=1r18 | SCENE= }} | | {{STRUCTURE_1r18| PDB=1r18 | SCENE= }} |
| | | | |
| - | '''Drosophila protein isoaspartyl methyltransferase with S-adenosyl-L-homocysteine'''
| + | ===Drosophila protein isoaspartyl methyltransferase with S-adenosyl-L-homocysteine=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Protein L-isoaspartyl methyltransferases (PIMT; EC 2.1.1.77) catalyze the S-adenosylmethionine-dependent methylation of L-isoaspartyl residues that arise spontaneously in proteins with age, thereby initiating a repair process that restores the normal backbone configuration to the damaged polypeptide. In Drosophila melanogaster, overexpression of PIMT in transgenic flies extends the normal life span, suggesting that protein damage can be a limiting factor in longevity. To understand structural features of the Drosophila PIMT (dPIMT) important for catalysis, the crystal structure of dPIMT was determined at a resolution of 2.2 A, and site-directed mutagenesis was used to identify the role of Ser-60 in catalysis. The core structure of dPIMT is similar to the modified nucleotide-binding fold observed in PIMTs from extreme thermophiles and humans. A striking difference of the dPIMT structure is the rotation of the C-terminal residues by 90 degrees relative to the homologous structures. Effectively, this displacement generates a more open conformation that allows greater solvent access to S-adenosylhomocysteine, which is almost completely buried in other PIMT structures. The enzyme may alternate between the open conformation found for dPIMT and the more closed conformations described for other PIMTs during its catalytic cycle, thereby allowing the exchange of substrates and products. Catalysis by dPIMT requires the side chain of the conserved, active site residue Ser-60, since substitution of this residue with Thr, Gln, or Ala reduces or abolishes the methylation of both protein and isoaspartyl peptide substrates.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14596598}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14596598 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_14596598}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Protein repair]] | | [[Category: Protein repair]] |
| | [[Category: S-adenosyl homocysteine]] | | [[Category: S-adenosyl homocysteine]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:57:02 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:25:17 2008'' |
Revision as of 18:25, 27 July 2008
Template:STRUCTURE 1r18
Drosophila protein isoaspartyl methyltransferase with S-adenosyl-L-homocysteine
Template:ABSTRACT PUBMED 14596598
About this Structure
1R18 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Catalytic implications from the Drosophila protein L-isoaspartyl methyltransferase structure and site-directed mutagenesis., Bennett EJ, Bjerregaard J, Knapp JE, Chavous DA, Friedman AM, Royer WE Jr, O'Connor CM, Biochemistry. 2003 Nov 11;42(44):12844-53. PMID:14596598
Page seeded by OCA on Sun Jul 27 21:25:17 2008
