1dcu
From Proteopedia
(New page: 200px<br /><applet load="1dcu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dcu, resolution 2.2Å" /> '''REDOX SIGNALING IN TH...) |
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| - | [[Image:1dcu.gif|left|200px]]<br /><applet load="1dcu" size=" | + | [[Image:1dcu.gif|left|200px]]<br /><applet load="1dcu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dcu, resolution 2.2Å" /> | caption="1dcu, resolution 2.2Å" /> | ||
'''REDOX SIGNALING IN THE CHLOROPLAST: STRUCTURE OF OXIDIZED PEA FRUCTOSE-1,6-BISPHOSPHATE PHOSPHATASE'''<br /> | '''REDOX SIGNALING IN THE CHLOROPLAST: STRUCTURE OF OXIDIZED PEA FRUCTOSE-1,6-BISPHOSPHATE PHOSPHATASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sunlight provides the energy source for the assimilation of carbon dioxide | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1DCU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http:// | + | 1DCU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cherfils, J.]] | [[Category: Cherfils, J.]] | ||
[[Category: Chiadmi, M.]] | [[Category: Chiadmi, M.]] | ||
| - | [[Category: Jacquot, J | + | [[Category: Jacquot, J P.]] |
[[Category: Miginiac-Maslow, M.]] | [[Category: Miginiac-Maslow, M.]] | ||
[[Category: Navaza, A.]] | [[Category: Navaza, A.]] | ||
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[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:20 2008'' |
Revision as of 10:15, 21 February 2008
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REDOX SIGNALING IN THE CHLOROPLAST: STRUCTURE OF OXIDIZED PEA FRUCTOSE-1,6-BISPHOSPHATE PHOSPHATASE
Overview
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.
About this Structure
1DCU is a Single protein structure of sequence from Pisum sativum. Active as Fructose-bisphosphatase, with EC number 3.1.3.11 Full crystallographic information is available from OCA.
Reference
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
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