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Crystal structure of T-protein of the Glycine Cleavage System

OverviewOverview

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 StructureAbout this Structure

1WOO 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.

ReferenceReference

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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 '''Crystal structure of T-protein of the Glycine Cleavage System'''<br />
 ==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.
+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==
-WOO 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 THL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WOO OCA].
+WOO 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=THL:'>THL</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=1WOO OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Ahn, H.J.]]
+[[Category: Ahn, H J.]]
-[[Category: Ha, J.Y.]]
+[[Category: Ha, J Y.]]
-[[Category: Kim, D.J.]]
+[[Category: Kim, D J.]]
-[[Category: Lee, H.H.]]
+[[Category: Lee, H H.]]
-[[Category: Suh, S.W.]]
+[[Category: Suh, S W.]]
 [[Category: THL]]
 [[Category: glycine cleavage system]]
@@ Line 24: / Line 24: @@
 [[Category: tetrahydrofolate]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:33:58 2007''
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