The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis

Protein Science : a Publication of the Protein Society
S PascarellaF Bossa

Abstract

We describe a model for the three-dimensional structure of E. coli serine hydroxymethyltransferase based on its sequence homology with other PLP enzymes of the alpha-family and whose tertiary structures are known. The model suggests that certain amino acid residues at the putative active site of the enzyme can adopt specific roles in the catalytic mechanism. These proposals were supported by analysis of the properties of a number of site-directed mutants. New active site features are also proposed for further experimental testing.

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Citations

Apr 13, 2000·The International Journal of Biochemistry & Cell Biology·N A RaoH S Savithri
Aug 21, 2013·BioMed Research International·Martino L Di SalvoH Tonie Wright
May 30, 2003·The Journal of Biological Chemistry·Tzu-Fun FuVerne Schirch

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