1eox | pdb_00001eox

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

SEDOHEPTULOSE-1,7-BISPHOSPHATASE FROM CHLAMYDOMONAS REINHARDTII (OXIDIZED FORM), THEORETICAL MODEL

spinqualitylabelsall models 1eox Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed 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. Identification of a potential redox-sensitive interdomain disulfide in the sedoheptulose bisphosphatase of Chlamydomonas reinhardtii.,Anderson LE, Huppe HC, Li AD, Stevens FJ Plant J. 1996 Sep;10(3):553-60. PMID:8811868 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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