Center for Structural Genomics of Infectious Diseases

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Structure of IDP01011

CSGID target: IDP01011
PDB Id: 3GBX (NCBI MMDB)
Authors: 'J.Osipiuk,B.Nocek,M.Zhou,J.Stam,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid)'
Responsible person: Jerzy Osipiuk
Responsible lab: Argonne National Laboratory
Deposition Date: Feb 20, 2009
Release Date: Mar 10, 2009

Description: Serine hydroxymethyltransferase (SHMT) is also called as serine aldolase. It is a pyridoxal-phosphate (PLP) dependent enzyme that plays a central role in the onecarbon metabolism. It catalyzes the reversible inter-conversion of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate, a key intermediate in the biosynthesis of purine, thymidine, choline, and methionine. In addition to this physiological reaction, SHMT has also been shown to catalyze THF-independent aldolytic cleavage, decarboxylation, racemization, and transamination reactions. The PLP dependent enzymes can be classified based on structure and sequence analysis into five major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), D-amino acid superfamily (fold type IV) and glycogen phophorylase family (fold type V). Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers and the mammalian enzyme forms a homotetramer. The importance of SHMT in DNA synthesis together with the high level of enzyme activity in rapidly proliferating cells has focused attention on SHMT as a potential drug target.
Functional assignment

Ligand code	Name	Ligand type
ACT
MSE		modified residue