1eji
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1EJI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]] with PLG and THF as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1EJI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]] with PLG and THF as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1]]. Structure known Active Sites: I, II, III and IV. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EJI OCA]]. |
==Reference== | ==Reference== | ||
Structure of a murine cytoplasmic serine hydroxymethyltransferase quinonoid ternary complex: evidence for asymmetric obligate dimers., Szebenyi DM, Liu X, Kriksunov IA, Stover PJ, Thiel DJ, Biochemistry. 2000 Nov 7;39(44):13313-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11063567 11063567] | Structure of a murine cytoplasmic serine hydroxymethyltransferase quinonoid ternary complex: evidence for asymmetric obligate dimers., Szebenyi DM, Liu X, Kriksunov IA, Stover PJ, Thiel DJ, Biochemistry. 2000 Nov 7;39(44):13313-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11063567 11063567] | ||
| + | [[Category: Glycine hydroxymethyltransferase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tetrahydrofolate]] | [[Category: tetrahydrofolate]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:25:58 2007'' |
Revision as of 08:21, 30 October 2007
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RECOMBINANT SERINE HYDROXYMETHYLTRANSFERASE (MOUSE)
Overview
Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate-dependent, enzyme that catalyzes the reversible conversion of serine and, tetrahydrofolate to glycine and methylenetetrahydrofolate. This reaction, generates single carbon units for purine, thymidine, and methionine, biosynthesis. The enzyme is a homotetramer comprising two obligate dimers, and four pyridoxal phosphate-bound active sites. The mammalian enzyme is, present in cells in both catalytically active and inactive forms. The, inactive form is a ternary complex that results from the binding of, glycine and 5-formyltetrahydrofolate polyglutamate, a slow tight-binding, inhibitor. The crystal structure of a close analogue of the inactive form, of murine cytoplasmic SHMT (cSHMT), lacking only the polyglutamate tail of, the ... [(full description)]
About this Structure
1EJI is a [Single protein] structure of sequence from [Mus musculus] with PLG and THF as [ligands]. Active as [Glycine hydroxymethyltransferase], with EC number [2.1.2.1]. Structure known Active Sites: I, II, III and IV. Full crystallographic information is available from [OCA].
Reference
Structure of a murine cytoplasmic serine hydroxymethyltransferase quinonoid ternary complex: evidence for asymmetric obligate dimers., Szebenyi DM, Liu X, Kriksunov IA, Stover PJ, Thiel DJ, Biochemistry. 2000 Nov 7;39(44):13313-23. PMID:11063567
Page seeded by OCA on Tue Oct 30 10:25:58 2007
