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

✍ Scribed by Stefano Pascarella; Sebastiana Angelaccio; Roberto Contestabile; Sonia Delle Fratte; Martino Di Salvo; Francesco Bossa

Publisher
Cold Spring Harbor Laboratory Press
Year
1998
Tongue
English
Weight
759 KB
Volume
7
Category
Article
ISSN
0961-8368

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✦ Synopsis

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 theα‐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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