1dl5
From Proteopedia
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[[Image:1dl5.gif|left|200px]] | [[Image:1dl5.gif|left|200px]] | ||
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'''PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE''' | '''PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE''' | ||
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==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/11080641 11080641] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11080641 11080641] | ||
| - | [[Category: Protein-L-isoaspartate(D-aspartate) O-methyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: Skinner, M M.]] | [[Category: Skinner, M M.]] | ||
[[Category: Walter, R L.]] | [[Category: Walter, R L.]] | ||
| - | [[Category: | + | [[Category: Deamidation]] |
| - | [[Category: | + | [[Category: Isoaspartyl residue]] |
| - | [[Category: | + | [[Category: Methyltransferase]] |
| - | [[Category: | + | [[Category: Post-translational modification]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 10:58, 2 May 2008
PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE
Overview
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.
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 Fri May 2 13:58:36 2008
