1kr5
From Proteopedia
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| - | [[Image:1kr5.gif|left|200px]] | + | [[Image:1kr5.gif|left|200px]] |
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| - | '''Crystal structure of human L-isoaspartyl methyltransferase''' | + | {{Structure |
| + | |PDB= 1kr5 |SIZE=350|CAPTION= <scene name='initialview01'>1kr5</scene>, resolution 2.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of human L-isoaspartyl methyltransferase''' | ||
| + | |||
| + | |||
| + | ==Overview== | ||
| + | The enzyme l-isoaspartyl methyltransferase initiates the repair of damaged proteins by recognizing and methylating isomerized and racemized aspartyl residues in aging proteins. The crystal structure of the human enzyme containing a bound S-adenosyl-l-homocysteine cofactor is reported here at a resolution of 2.1 A. A comparison of the human enzyme to homologs from two other species reveals several significant differences among otherwise similar structures. In all three structures, we find that three conserved charged residues are buried in the protein interior near the active site. Electrostatics calculations suggest that these buried charges might make significant contributions to the energetics of binding the charged S-adenosyl-l-methionine cofactor and to catalysis. We suggest a possible structural explanation for the observed differences in reactivity toward the structurally similar l-isoaspartyl and d-aspartyl residues in the human, archael, and eubacterial enzymes. Finally, the human structure reveals that the known genetic polymorphism at residue 119 (Val/Ile) maps to an exposed region away from the active site. | ||
==About this Structure== | ==About this Structure== | ||
| - | 1KR5 is a [ | + | 1KR5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KR5 OCA]. |
| + | |||
| + | ==Reference== | ||
| + | Crystal structure of human L-isoaspartyl methyltransferase., Ryttersgaard C, Griffith SC, Sawaya MR, MacLaren DC, Clarke S, Yeates TO, J Biol Chem. 2002 Mar 22;277(12):10642-6. Epub 2002 Jan 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11792715 11792715] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-L-isoaspartate(D-aspartate) O-methyltransferase]] | [[Category: Protein-L-isoaspartate(D-aspartate) O-methyltransferase]] | ||
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[[Category: rossmann-fold doubly-wound-alpha-beta-alpha-sandwich]] | [[Category: rossmann-fold doubly-wound-alpha-beta-alpha-sandwich]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:21:04 2008'' |
Revision as of 10:21, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Ligands: | |||||||
| Activity: | Protein-L-isoaspartate(D-aspartate) O-methyltransferase, with EC number 2.1.1.77 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human L-isoaspartyl methyltransferase
Overview
The enzyme l-isoaspartyl methyltransferase initiates the repair of damaged proteins by recognizing and methylating isomerized and racemized aspartyl residues in aging proteins. The crystal structure of the human enzyme containing a bound S-adenosyl-l-homocysteine cofactor is reported here at a resolution of 2.1 A. A comparison of the human enzyme to homologs from two other species reveals several significant differences among otherwise similar structures. In all three structures, we find that three conserved charged residues are buried in the protein interior near the active site. Electrostatics calculations suggest that these buried charges might make significant contributions to the energetics of binding the charged S-adenosyl-l-methionine cofactor and to catalysis. We suggest a possible structural explanation for the observed differences in reactivity toward the structurally similar l-isoaspartyl and d-aspartyl residues in the human, archael, and eubacterial enzymes. Finally, the human structure reveals that the known genetic polymorphism at residue 119 (Val/Ile) maps to an exposed region away from the active site.
About this Structure
1KR5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human L-isoaspartyl methyltransferase., Ryttersgaard C, Griffith SC, Sawaya MR, MacLaren DC, Clarke S, Yeates TO, J Biol Chem. 2002 Mar 22;277(12):10642-6. Epub 2002 Jan 15. PMID:11792715
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