PDBsum entry 1eox

Carbohydrate metabolism

PDB id: 1eox

Contents

Protein chain

315 a.a.

Theoretical model

PDB id:

1eox

Name:

Carbohydrate metabolism

Title:

Sedoheptulose-1,7-bisphosphatase from chlamydomonas reinhardtii (oxidized form), theoretical model

Structure:

Sedoheptulose-1,7-bisphosphatase. Chain: null. Biological_unit: homodimer. Other_details: oxidized

Source:

Chlamydomonas reinhardtii. Strain: cw406

Authors:

L.E.Anderson,H.C.Huppe,A.D.Li,F.J.Stevens

Key ref:

L.E.Anderson et al. (1996). Identification of a potential redox-sensitive interdomain disulfide in the sedoheptulose bisphosphatase of Chlamydomonas reinhardtii. Plant J, 10, 553-560. PubMed id: 8811868

Date:

10-Jul-96 Release date: 11-Jan-97

Protein chain

No UniProt id for this chain

Struc: 315 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.3.37 - sedoheptulose-bisphosphatase.
• Pathway: Calvin Cycle
• Reaction: D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-phosphate + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Plant J 10:553-560 (1996)

PubMed id: 8811868

Identification of a potential redox-sensitive interdomain disulfide in the sedoheptulose bisphosphatase of Chlamydomonas reinhardtii.

L.E.Anderson, H.C.Huppe, A.D.Li, F.J.Stevens.

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.