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| <StructureSection load='3thg' size='340' side='right'caption='[[3thg]], [[Resolution|resolution]] 1.88Å' scene=''> | | <StructureSection load='3thg' size='340' side='right'caption='[[3thg]], [[Resolution|resolution]] 1.88Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3thg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Creosote_bush Creosote bush]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3thg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Larrea_tridentata Larrea tridentata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THG FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66636 Creosote bush])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3thg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thg OCA], [https://pdbe.org/3thg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thg RCSB], [https://www.ebi.ac.uk/pdbsum/3thg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thg 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=3thg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thg OCA], [https://pdbe.org/3thg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thg RCSB], [https://www.ebi.ac.uk/pdbsum/3thg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thg ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/RCA1_LARTR RCA1_LARTR]] Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure.
| + | [https://www.uniprot.org/uniprot/RCA1_LARTR RCA1_LARTR] Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure. |
- | <div style="background-color:#fffaf0;">
| + | |
- | == Publication Abstract from PubMed ==
| + | |
- | The rapid release of tight-binding inhibitors from dead-end ribulose-bisphosphate carboxylase/oxygenase (Rubisco) complexes requires the activity of Rubisco activase, an AAA+ ATPase that utilizes chemo-mechanical energy to catalyze the reactivation of Rubisco. Activase is thought to play a central role in coordinating the rate of CO(2) fixation with the light reactions of photosynthesis. Here, we present a 1.9 A crystal structure of the C-domain core of creosote activase. The fold consists of a canonical four-helix bundle, from which a paddle-like extension protrudes that entails a nine-turn helix lined by an irregularly structured peptide strand. The residues Lys-313 and Val-316 involved in the species-specific recognition of Rubisco are located near the tip of the paddle. An ionic bond between Lys-313 and Glu-309 appears to stabilize the glycine-rich end of the helix. Structural superpositions onto the distant homolog FtsH imply that the paddles extend away from the hexameric toroid in a fan-like fashion, such that the hydrophobic sides of each blade bearing Trp-302 are facing inward and the polar sides bearing Lys-313 and Val-316 are facing outward. Therefore, we speculate that upon binding, the activase paddles embrace the Rubisco cylinder by placing their hydrophobic patches near the partner protein. This model suggests that conformational adjustments at the remote end of the paddle may relate to selectivity in recognition, rather than specific ionic contacts involving Lys-313. Additionally, the superpositions predict that the catalytically critical Arg-293 does not interact with the bound nucleotide. Hypothetical ring-ring stacking and peptide threading models for Rubisco reactivation are briefly discussed.
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- | Atomic resolution x-ray structure of the substrate recognition domain of higher plant ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase.,Henderson JN, Kuriata AM, Fromme R, Salvucci ME, Wachter RM J Biol Chem. 2011 Oct 14;286(41):35683-8. Epub 2011 Aug 31. PMID:21880724<ref>PMID:21880724</ref>
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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- | </div>
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- | <div class="pdbe-citations 3thg" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[RuBisCO 3D structures|RuBisCO 3D structures]] | | *[[RuBisCO 3D structures|RuBisCO 3D structures]] |
- | == References == | |
- | <references/> | |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Creosote bush]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Fromme, R]] | + | [[Category: Larrea tridentata]] |
- | [[Category: Henderson, J N]] | + | [[Category: Fromme R]] |
- | [[Category: Kuriata, A M]]
| + | [[Category: Henderson JN]] |
- | [[Category: Salvucci, M E]]
| + | [[Category: Kuriata AM]] |
- | [[Category: Wachter, R M]]
| + | [[Category: Salvucci ME]] |
- | [[Category: Aaa+]] | + | [[Category: Wachter RM]] |
- | [[Category: Atpase]] | + | |
- | [[Category: Chloroplast stroma]] | + | |
- | [[Category: Four-helix bundle]] | + | |
- | [[Category: Protein binding]]
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- | [[Category: Rubisco reactivation]]
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