1eji
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(New page: 200px<br /> <applet load="1eji" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eji, resolution 2.90Å" /> '''RECOMBINANT SERINE ...)
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Revision as of 14:03, 29 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 [[1]], with EC number [2.1.2.1]. 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
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