1eoy: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:1eoy.png|left|200px]]
-<!--
+==SEDOHEPTULOSE-1,7-BISPHOSPHATASE FROM CHLAMYDOMONAS REINHARDTII (REDUCED FORM), THEORETICAL MODEL==
-The line below this paragraph, containing "STRUCTURE_1eoy", creates the "Structure Box" on the page.
+<StructureSection load='1eoy' size='340' side='right'caption='[[1eoy]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EOY FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=1eoy FirstGlance], [https://www.ebi.ac.uk/pdbsum/1eoy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eoy ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_1eoy|  PDB=1eoy  |  SCENE=  }}
+<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.
-===SEDOHEPTULOSE-1,7-BISPHOSPHATASE FROM CHLAMYDOMONAS REINHARDTII (REDUCED FORM), THEORETICAL MODEL===
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_8811868}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1eoy" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 8811868 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_8811868}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOY OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:8811868</ref><references group="xtra"/>
 [[Category: Anderson, L E]]
 [[Category: Huppe, H C]]
 [[Category: Li, A D]]
 [[Category: Stevens, F J]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 08:57:30 2010''