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| - | [[Image:2idj.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2idj| PDB=2idj | SCENE= }} | | {{STRUCTURE_2idj| PDB=2idj | SCENE= }} |
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| - | '''Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form'''
| + | ===Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form=== |
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| - | ==Overview==
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| - | Glycine N-methyltransferase (GNMT) is a key regulatory enzyme in methyl group metabolism. It is abundant in the liver, where it uses excess S-adenosylmethionine (AdoMet) to methylate glycine to N-methylglycine (sarcosine) and produces S-adenosylhomocysteine (AdoHcy), thereby controlling the methylating potential of the cell. GNMT also links utilization of preformed methyl groups, in the form of methionine, to their de novo synthesis, because it is inhibited by a specific form of folate, 5-methyltetrahydrofolate. Although the structure of the enzyme has been elucidated by x-ray crystallography of the apoenzyme and in the presence of the substrate, the location of the folate inhibitor in the tetrameric structure has not been identified. We report here for the first time the crystal structure of rat GNMT complexed with 5-methyltetrahydrofolate. In the GNMT-folate complex, two folate binding sites were located in the intersubunit areas of the tetramer. Each folate binding site is formed primarily by two 1-7 N-terminal regions of one pair of subunits and two 205-218 regions of the other pair of subunits. Both the pteridine and p-aminobenzoyl rings are located in the hydrophobic cavities formed by Tyr5, Leu207, and Met215 residues of all subunits. Binding experiments in solution also confirm that one GNMT tetramer binds two folate molecules. For the enzymatic reaction to take place, the N-terminal fragments of GNMT must have a significant degree of conformational freedom to provide access to the active sites. The presence of the folate in this position provides a mechanism for its inhibition.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17158459}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17158459 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17158459}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Glycine n-methyltransferase]] | | [[Category: Glycine n-methyltransferase]] |
| | [[Category: Rat]] | | [[Category: Rat]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:22:27 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:19:14 2008'' |
Revision as of 02:19, 28 July 2008
Template:STRUCTURE 2idj
Crystal Structure of Rat Glycine N-Methyltransferase Apoprotein, Monoclinic Form
Template:ABSTRACT PUBMED 17158459
About this Structure
2IDJ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
5-methyltetrahydrofolate is bound in intersubunit areas of rat liver folate-binding protein glycine N-methyltransferase., Luka Z, Pakhomova S, Loukachevitch LV, Egli M, Newcomer ME, Wagner C, J Biol Chem. 2007 Feb 9;282(6):4069-75. Epub 2006 Dec 7. PMID:17158459
Page seeded by OCA on Mon Jul 28 05:19:14 2008
