4uav: Difference between revisions
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==Crystal structure of CbbY (AT3G48420) from Arabidobsis thaliana== | |||
<StructureSection load='4uav' size='340' side='right'caption='[[4uav]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uav]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UAV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4uav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uav OCA], [https://pdbe.org/4uav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uav RCSB], [https://www.ebi.ac.uk/pdbsum/4uav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uav ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CBBY_ARATH CBBY_ARATH] Highly selective xylulose-1,5-bisphosphate (XuBP) phosphatase. Shows also activity towards ribulose-1,5-bisphosphate (RuBP) and fructose-1,6-bisphosphate (FBP), but not towards fructose-6-phosphate (F6P) or ribulose-5-phosphate (Ru5P) (PubMed:27246049). Degrades xylulose-1,5-bisphosphate, a potent inhibitor of rubisco produced by the rubisco itself (PubMed:27246049).<ref>PMID:27246049</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the conversion of atmospheric carbon dioxide into organic compounds in photosynthetic organisms. Alongside carboxylating the five-carbon sugar ribulose-1,5-bisphosphate (RuBP)(1-3), Rubisco produces a small amount of xylulose-1,5-bisphosphate (XuBP), a potent inhibitor of Rubisco(4). The AAA+ protein Rubisco activase removes XuBP from the active site of Rubisco in an ATP-dependent process(5,6). However, free XuBP rapidly rebinds to Rubisco, perpetuating its inhibitory effect. Here, we combine biochemical and structural analyses to show that the CbbY protein of the photosynthetic bacterium Rhodobacter sphaeroides and Arabidopsis thaliana is a highly selective XuBP phosphatase. We also show that CbbY converts XuBP to the non-inhibitory compound xylulose-5-phosphate, which is recycled back to RuBP. We solve the crystal structures of CbbY from R. sphaeroides and A. thaliana, and through mutational analysis show that the cap domain of the protein confers the selectivity for XuBP over RuBP. Finally, in vitro experiments with CbbY from R. sphaeroides reveal that CbbY cooperates with Rubisco activase to prevent a detrimental build-up of XuBP at the Rubisco active site. We suggest that CbbY, which is conserved in algae and plants, is an important component of the cellular machinery that has evolved to deal with the shortcomings of the ancient enzyme Rubisco. | |||
Degradation of potent Rubisco inhibitor by selective sugar phosphatase.,Bracher A, Sharma A, Starling-Windhof A, Hartl FU, Hayer-Hartl M Nat Plants. 2015 Jan 8;1:14002. doi: 10.1038/nplants.2014.2. PMID:27246049<ref>PMID:27246049</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bracher | <div class="pdbe-citations 4uav" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | |||
[[Category: Bracher A]] | |||
[[Category: Hartl FU]] | |||
[[Category: Hayer-Hartl M]] | |||
[[Category: Sharma A]] | |||
[[Category: Starling-Windhof A]] | |||
Latest revision as of 15:27, 20 December 2023
Crystal structure of CbbY (AT3G48420) from Arabidobsis thalianaCrystal structure of CbbY (AT3G48420) from Arabidobsis thaliana
Structural highlights
FunctionCBBY_ARATH Highly selective xylulose-1,5-bisphosphate (XuBP) phosphatase. Shows also activity towards ribulose-1,5-bisphosphate (RuBP) and fructose-1,6-bisphosphate (FBP), but not towards fructose-6-phosphate (F6P) or ribulose-5-phosphate (Ru5P) (PubMed:27246049). Degrades xylulose-1,5-bisphosphate, a potent inhibitor of rubisco produced by the rubisco itself (PubMed:27246049).[1] Publication Abstract from PubMedRibulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the conversion of atmospheric carbon dioxide into organic compounds in photosynthetic organisms. Alongside carboxylating the five-carbon sugar ribulose-1,5-bisphosphate (RuBP)(1-3), Rubisco produces a small amount of xylulose-1,5-bisphosphate (XuBP), a potent inhibitor of Rubisco(4). The AAA+ protein Rubisco activase removes XuBP from the active site of Rubisco in an ATP-dependent process(5,6). However, free XuBP rapidly rebinds to Rubisco, perpetuating its inhibitory effect. Here, we combine biochemical and structural analyses to show that the CbbY protein of the photosynthetic bacterium Rhodobacter sphaeroides and Arabidopsis thaliana is a highly selective XuBP phosphatase. We also show that CbbY converts XuBP to the non-inhibitory compound xylulose-5-phosphate, which is recycled back to RuBP. We solve the crystal structures of CbbY from R. sphaeroides and A. thaliana, and through mutational analysis show that the cap domain of the protein confers the selectivity for XuBP over RuBP. Finally, in vitro experiments with CbbY from R. sphaeroides reveal that CbbY cooperates with Rubisco activase to prevent a detrimental build-up of XuBP at the Rubisco active site. We suggest that CbbY, which is conserved in algae and plants, is an important component of the cellular machinery that has evolved to deal with the shortcomings of the ancient enzyme Rubisco. Degradation of potent Rubisco inhibitor by selective sugar phosphatase.,Bracher A, Sharma A, Starling-Windhof A, Hartl FU, Hayer-Hartl M Nat Plants. 2015 Jan 8;1:14002. doi: 10.1038/nplants.2014.2. PMID:27246049[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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