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'''Crystal Structure of T-protein of the Glycine Cleavage System''' | '''Crystal Structure of T-protein of the Glycine Cleavage System''' | ||
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[[Category: Lee, H H.]] | [[Category: Lee, H H.]] | ||
[[Category: Suh, S W.]] | [[Category: Suh, S W.]] | ||
[[Category: | [[Category: Aminomethyltransferase]] | ||
[[Category: | [[Category: T-protein]] | ||
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Revision as of 13:57, 3 May 2008
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
1WOS is a Single protein structure of sequence from Thermotoga maritima. 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 Page seeded by OCA on Sat May 3 13:57:30 2008