1dcu
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dcu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCU FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dcu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCU FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcu OCA], [https://pdbe.org/1dcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcu RCSB], [https://www.ebi.ac.uk/pdbsum/1dcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcu ProSAT]</span></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=1dcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcu OCA], [https://pdbe.org/1dcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcu RCSB], [https://www.ebi.ac.uk/pdbsum/1dcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/F16P1_PEA F16P1_PEA] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dcu ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dcu ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Sunlight provides the energy source for the assimilation of carbon dioxide by photosynthesis, but it also provides regulatory signals that switch on specific sets of enzymes involved in the alternation of light and dark metabolisms in chloroplasts. Capture of photons by chlorophyll pigments triggers redox cascades that ultimately activate target enzymes via the reduction of regulatory disulfide bridges by thioredoxins. Here we report the structure of the oxidized, low-activity form of chloroplastic fructose-1, 6-bisphosphate phosphatase (FBPase), one of the four enzymes of the Calvin cycle whose activity is redox-regulated by light. The regulation is of allosteric nature, with a disulfide bridge promoting the disruption of the catalytic site across a distance of 20 A. Unexpectedly, regulation of plant FBPases by thiol-disulfide interchange differs in every respect from the regulation of mammalian gluconeogenic FBPases by AMP. We also report a second crystal form of oxidized FBPase whose tetrameric structure departs markedly from D(2) symmetry, a rare event in oligomeric structures, and the structure of a constitutively active mutant that is unable to form the regulatory disulfide bridge. Altogether, these structures provide a structural basis for redox regulation in the chloroplast. | ||
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| - | Redox signalling in the chloroplast: structure of oxidized pea fructose-1,6-bisphosphate phosphatase.,Chiadmi M, Navaza A, Miginiac-Maslow M, Jacquot JP, Cherfils J EMBO J. 1999 Dec 1;18(23):6809-15. PMID:10581254<ref>PMID:10581254</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1dcu" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]] | *[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Fructose-bisphosphatase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pisum sativum]] | [[Category: Pisum sativum]] | ||
| - | [[Category: Cherfils | + | [[Category: Cherfils J]] |
| - | [[Category: Chiadmi | + | [[Category: Chiadmi M]] |
| - | [[Category: Jacquot | + | [[Category: Jacquot JP]] |
| - | [[Category: Miginiac-Maslow | + | [[Category: Miginiac-Maslow M]] |
| - | [[Category: Navaza | + | [[Category: Navaza A]] |
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Revision as of 09:49, 20 March 2024
REDOX SIGNALING IN THE CHLOROPLAST: STRUCTURE OF OXIDIZED PEA FRUCTOSE-1,6-BISPHOSPHATE PHOSPHATASE
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