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| - | [[Image:1wsr.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1wsr| PDB=1wsr | SCENE= }} | | {{STRUCTURE_1wsr| PDB=1wsr | SCENE= }} |
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| - | '''Crystal Structure of Human T-protein of Glycine Cleavage System'''
| + | ===Crystal Structure of Human T-protein of Glycine Cleavage System=== |
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| - | ==Overview==
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| - | T-protein, a component of the glycine cleavage system, catalyzes the formation of ammonia and 5,10-methylenetetrahydrofolate from the aminomethyl moiety of glycine attached to the lipoate cofactor of H-protein. Several mutations in the human T-protein gene cause non-ketotic hyperglycinemia. To gain insights into the effect of disease-causing mutations and the catalytic mechanism at the molecular level, crystal structures of human T-protein in free form and that bound to 5-methyltetrahydrofolate (5-CH3-H4folate) have been determined at 2.0 A and 2.6 A resolution, respectively. The overall structure consists of three domains arranged in a cloverleaf-like structure with the central cavity, where 5-CH3-H4folate is bound in a kinked shape with the pteridine group deeply buried into the hydrophobic pocket and the glutamyl group pointed to the C-terminal side surface. Most of the disease-related residues cluster around the cavity, forming extensive hydrogen bonding networks. These hydrogen bonding networks are employed in holding not only the folate-binding space but also the positions and the orientations of alpha-helix G and the following loop in the middle region, which seems to play a pivotal role in the T-protein catalysis. Structural and mutational analyses demonstrated that Arg292 interacts through water molecules with the folate polyglutamate tail, and that the invariant Asp101, located close to the N10 group of 5-CH3-H4folate, might play a key role in the initiation of the catalysis by increasing the nucleophilic character of the N10 atom of the folate substrate for the nucleophilic attack on the aminomethyl lipoate intermediate. A clever mechanism of recruiting the aminomethyl lipoate arm to the reaction site seems to function as a way of avoiding the release of toxic formaldehyde.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16051266}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16051266 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16051266}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Aminomethyl transferase]] | | [[Category: Aminomethyl transferase]] |
| | [[Category: Glycine-cleavage sytem]] | | [[Category: Glycine-cleavage sytem]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:05:26 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:14:24 2008'' |
Revision as of 15:14, 27 July 2008
Template:STRUCTURE 1wsr
Crystal Structure of Human T-protein of Glycine Cleavage System
Template:ABSTRACT PUBMED 16051266
About this Structure
1WSR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia., Okamura-Ikeda K, Hosaka H, Yoshimura M, Yamashita E, Toma S, Nakagawa A, Fujiwara K, Motokawa Y, Taniguchi H, J Mol Biol. 2005 Sep 2;351(5):1146-59. PMID:16051266
Page seeded by OCA on Sun Jul 27 18:14:24 2008
