1wor
From Proteopedia
(New page: 200px<br /><applet load="1wor" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wor, resolution 1.95Å" /> '''Crystal Structure of...) |
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| - | [[Image:1wor.gif|left|200px]]<br /><applet load="1wor" size=" | + | [[Image:1wor.gif|left|200px]]<br /><applet load="1wor" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wor, resolution 1.95Å" /> | caption="1wor, resolution 1.95Å" /> | ||
'''Crystal Structure of T-protein of the Glycine Cleavage System'''<br /> | '''Crystal Structure of T-protein of the Glycine Cleavage System'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The glycine cleavage system catalyzes the oxidative decarboxylation of | + | The glycine cleavage system catalyzes the oxidative decarboxylation of glycine in bacteria and in mitochondria of animals and plants. Its deficiency in human causes nonketotic hyperglycinemia, an inborn error of glycine metabolism. T-protein, one of the four components of the glycine cleavage system,is a tetrahydrofolate dependent aminomethyltransferase. It catalyzes the transfer of the methylene carbon unit to tetrahydrofolate from the methylamine group covalently attached to the lipoamide arm of H-protein. To gain insight into the T-protein function at the molecular level, we have determined the first crystal structure of T-protein from Thermotoga maritima by the multiwavelength anomalous diffraction method of x-ray crystallography and refined four structures: the apoform; the tetrahydrofolate complex; the folinic acid complex; and the lipoic acid complex. The overall fold of T-protein is similar to that of the C-terminal tetrahydrofolate-binding region (residues 421-830) of Arthrobacter globiformis dimethylglycine oxidase. Tetrahydrofolate (or folinic acid) is bound near the center of the tripartite T-protein. Lipoic acid is bound adjacent to the tetrahydrofolate binding pocket, thus defining the interaction surface for H-protein binding. A homology model of the human T-protein provides the structural framework for understanding the molecular mechanisms underlying the development of nonketotic hyperglycinemia due to missense mutations of the human T-protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1WOR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with RED as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] Full crystallographic information is available from [http:// | + | 1WOR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=RED:'>RED</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aminomethyltransferase Aminomethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.10 2.1.2.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WOR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Ahn, H | + | [[Category: Ahn, H J.]] |
| - | [[Category: Ha, J | + | [[Category: Ha, J Y.]] |
| - | [[Category: Kim, D | + | [[Category: Kim, D J.]] |
| - | [[Category: Lee, H | + | [[Category: Lee, H H.]] |
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
[[Category: RED]] | [[Category: RED]] | ||
[[Category: aminomethyltransferase]] | [[Category: aminomethyltransferase]] | ||
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[[Category: t-protein]] | [[Category: t-protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:36 2008'' |
Revision as of 13:46, 21 February 2008
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Crystal Structure of T-protein of the Glycine Cleavage System
Overview
The glycine cleavage system catalyzes the oxidative decarboxylation of glycine in bacteria and in mitochondria of animals and plants. Its deficiency in human causes nonketotic hyperglycinemia, an inborn error of glycine metabolism. T-protein, one of the four components of the glycine cleavage system,is a tetrahydrofolate dependent aminomethyltransferase. It catalyzes the transfer of the methylene carbon unit to tetrahydrofolate from the methylamine group covalently attached to the lipoamide arm of H-protein. To gain insight into the T-protein function at the molecular level, we have determined the first crystal structure of T-protein from Thermotoga maritima by the multiwavelength anomalous diffraction method of x-ray crystallography and refined four structures: the apoform; the tetrahydrofolate complex; the folinic acid complex; and the lipoic acid complex. The overall fold of T-protein is similar to that of the C-terminal tetrahydrofolate-binding region (residues 421-830) of Arthrobacter globiformis dimethylglycine oxidase. Tetrahydrofolate (or folinic acid) is bound near the center of the tripartite T-protein. Lipoic acid is bound adjacent to the tetrahydrofolate binding pocket, thus defining the interaction surface for H-protein binding. A homology model of the human T-protein provides the structural framework for understanding the molecular mechanisms underlying the development of nonketotic hyperglycinemia due to missense mutations of the human T-protein.
About this Structure
1WOR is a Single protein structure of sequence from Thermotoga maritima with as ligand. Active as Aminomethyltransferase, with EC number 2.1.2.10 Full crystallographic information is available from OCA.
Reference
Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia., Lee HH, Kim DJ, Ahn HJ, Ha JY, Suh SW, J Biol Chem. 2004 Nov 26;279(48):50514-23. Epub 2004 Sep 7. PMID:15355973
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