1cj0
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(New page: 200px<br /><applet load="1cj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cj0, resolution 2.80Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 10:23, 20 November 2007
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CRYSTAL STRUCTURE OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE AT 2.8 ANGSTROM RESOLUTION
Overview
Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage, of serine to form glycine and single carbon groups that are essential for, many biosynthetic pathways. SHMT requires both pyridoxal phosphate (PLP), and tetrahydropteroylpolyglutamate (H4PteGlun) as cofactors, the latter as, a carrier of the single carbon group. We describe here the crystal, structure at 2.8 A resolution of rabbit cytosolic SHMT (rcSHMT) in two, forms: one with the PLP covalently bound as an aldimine to the, Nepsilon-amino group of the active site lysine and the other with the, aldimine reduced to a secondary amine. The rcSHMT structure closely, resembles the structure of human SHMT, confirming its similarity to the, alpha-class of PLP enzymes. The structures reported here further permit, identification of changes in the PLP group that accompany formation of the, geminal diamine complex, the first intermediate in the reaction pathway., On the basis of the current mechanism derived from solution studies and, the properties of site mutants, we are able to model the binding of both, the serine substrate and the H4PteGlun cofactor. This model explains the, properties of several site mutants of SHMT and offers testable hypotheses, for a more detailed mechanism of this enzyme.
About this Structure
1CJ0 is a Single protein structure of sequence from Oryctolagus cuniculus with PLP as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 A resolution: mechanistic implications., Scarsdale JN, Kazanina G, Radaev S, Schirch V, Wright HT, Biochemistry. 1999 Jun 29;38(26):8347-58. PMID:10387080
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