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{{Theoretical_model}} | {{Theoretical_model}} | ||
==SEDOHEPTULOSE-1,7-BISPHOSPHATASE FROM CHLAMYDOMONAS REINHARDTII (OXIDIZED FORM), THEORETICAL MODEL== | |||
<StructureSection load='1eox' size='340' side='right'caption='[[1eox]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EOX FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eox FirstGlance], [https://www.ebi.ac.uk/pdbsum/1eox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eox ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:8811868</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1eox" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Theoretical Model]] | ||
[[Category: Large Structures]] | |||
== | |||
< | |||
[[Category: Anderson, L E]] | [[Category: Anderson, L E]] | ||
[[Category: Huppe, H C]] | [[Category: Huppe, H C]] | ||
[[Category: Li, A D]] | [[Category: Li, A D]] | ||
[[Category: Stevens, F J]] | [[Category: Stevens, F J]] | ||
Latest revision as of 12:40, 21 July 2021
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SEDOHEPTULOSE-1,7-BISPHOSPHATASE FROM CHLAMYDOMONAS REINHARDTII (OXIDIZED FORM), THEORETICAL MODELSEDOHEPTULOSE-1,7-BISPHOSPHATASE FROM CHLAMYDOMONAS REINHARDTII (OXIDIZED FORM), THEORETICAL MODEL
Structural highlights
Publication Abstract from PubMedIn 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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