Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli).

@article{Juers2009DirectAI,
  title={Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli).},
  author={Douglas H Juers and Beatrice Rob and Megan L Dugdale and Nastaron Rahimzadeh and Clarence Giang and Michelle Lee and Brian W. Matthews and Reuben E Huber},
  journal={Protein science : a publication of the Protein Society},
  year={2009},
  volume={18 6},
  pages={1281-92}
}
The active site of ss-galactosidase (E. coli) contains a Mg(2+) ion ligated by Glu-416, His-418 and Glu-461 plus three water molecules. A Na(+) ion binds nearby. To better understand the role of the active site Mg(2+) and its ligands, His-418 was substituted with Asn, Glu and Phe. The Asn-418 and Glu-418 variants could be crystallized and the structures were shown to be very similar to native enzyme. The Glu-418 variant showed increased mobility of some residues in the active site, which… CONTINUE READING

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