PDBsum entry 1eox

Carbohydrate metabolism

PDB id: 1eox

Contents

Protein chain

315 a.a.

References listed in PDB file

Key reference

• Title: Identification of a potential redox-Sensitive interdomain disulfide in the sedoheptulose bisphosphatase of chlamydomonas reinhardtii.
• Authors: L.E.Anderson, H.C.Huppe, A.D.Li, F.J.Stevens.
• Ref.: Plant J, 1996, 10, 553-560.
• PubMed id: 8811868

Abstract

In the stimulated three-dimensional structure of the Chlamydomonas reinhardtii sedoheptulose bisphosphatase (EC 3.1.3.37) there are two cysteine residues close enough to one another to form a redox-sensitive disulfide bond which would cross-link the nucleotide and carbon substrate domains. Examination of the redox modulation of this sedoheptulose bisphosphatase confirms that it resembles the higher plant enzyme in being activated by reduction. In the wheat and Arabidopsis enzymes, for which there is sequence information and which, like the Chlamydomonas enzyme, can be modeled, both redox-sensitive Cys residues appear to be located on the regulatory nucleotide-binding domain. Apparently different Cys residues are involved in modulation in the algal and higher plant sedoheptulose bisphosphatases.