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| - | [[Image:1dl5.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1dl5.png|left|200px]] |
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| | {{STRUCTURE_1dl5| PDB=1dl5 | SCENE= }} | | {{STRUCTURE_1dl5| PDB=1dl5 | SCENE= }} |
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| - | '''PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE'''
| + | ===PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE=== |
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| - | ==Overview==
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| - | BACKGROUND: Formation of isoaspartyl residues is one of several processes that damage proteins as they age. Protein L-isoaspartate (D-aspartate) O-methyltransferase (PIMT) is a conserved and nearly ubiquitous enzyme that catalyzes the repair of proteins damaged by isoaspartyl formation. RESULTS: We have determined the first structure of a PIMT from crystals of the T. maritima enzyme complexed to S-adenosyl-L-homocysteine (AdoHcy) and refined it to 1.8 A resolution. Although PIMT forms one structural unit, the protein can be divided functionally into three subdomains. The central subdomain closely resembles other S-adenosyl-L-methionine-dependent methyltransferases but bears a striking alteration of topological connectivity, which is not shared by any other member of this family. Rather than arranged as a mixed beta sheet with topology 6 upward arrow7 downward arrow5 upward arrow4 upward arrow1 upward arrow2 upward arrow3 upward arrow, the central sheet of PIMT is reorganized to 7 upward arrow6 downward arrow5 upward arrow4 upward arrow1 upward arrow2 upward arrow3 upward arrow. AdoHcy is largely buried between the N-terminal and central subdomains by a conserved and largely hydrophobic loop on one rim of the binding cleft, and a conserved Ser/Thr-rich beta strand on the other. The Ser/Thr-rich strand may provide hydrogen bonds for specific interactions with isoaspartyl substrates. The side chain of Ile-206, a conserved residue, crosses the cleft, restricting access to the donor methyl group to a deep well, the putative isoaspartyl methyl acceptor site. CONCLUSIONS: The structure of PIMT reveals a unique modification of the methyltransferase fold along with a site for specific recognition of isoaspartyl substrates. The sequence conservation among PIMTs suggests that the current structure should prove a reliable model for understanding the repair of isoaspartyl damage in all organisms.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11080641}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11080641 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11080641}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Post-translational modification]] | | [[Category: Post-translational modification]] |
| | [[Category: Protein repair]] | | [[Category: Protein repair]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:58:36 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:14:13 2008'' |
Revision as of 20:14, 30 June 2008
Template:STRUCTURE 1dl5
PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE
Template:ABSTRACT PUBMED 11080641
About this Structure
1DL5 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Crystal structure of protein isoaspartyl methyltransferase: a catalyst for protein repair., Skinner MM, Puvathingal JM, Walter RL, Friedman AM, Structure. 2000 Nov 15;8(11):1189-201. PMID:11080641
Page seeded by OCA on Mon Jun 30 23:14:13 2008
