|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3syk' size='340' side='right'caption='[[3syk]], [[Resolution|resolution]] 3.08Å' scene=''> | | <StructureSection load='3syk' size='340' side='right'caption='[[3syk]], [[Resolution|resolution]] 3.08Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3syk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SYK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3syk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SYK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.08Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3syl|3syl]], [[3zuh|3zuh]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbbX, RSKD131_2679 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907])</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=3syk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3syk OCA], [https://pdbe.org/3syk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3syk RCSB], [https://www.ebi.ac.uk/pdbsum/3syk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3syk 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=3syk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3syk OCA], [https://pdbe.org/3syk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3syk RCSB], [https://www.ebi.ac.uk/pdbsum/3syk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3syk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CBBX_RHOSH CBBX_RHOSH]] Seems to be necessary for the expression of RuBisCO.
| + | [https://www.uniprot.org/uniprot/CBBX_CERSP CBBX_CERSP] ATPase involved in the activation of red-type RuBisCo (ribulose-1,5-bisphosphate carboxylase/oxygenase), which tends to form inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP) (PubMed:22048315, PubMed:27872295). Catalyzes the release of RuBP from inhibited RuBisCo in an ATP-dependent manner (PubMed:22048315, PubMed:27872295). Activation of RuBisCO involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure (PubMed:22048315, PubMed:27872295).<ref>PMID:22048315</ref> <ref>PMID:27872295</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhodococcus capsulatus molisch 1907]] | + | [[Category: Cereibacter sphaeroides]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bracher, A]] | + | [[Category: Bracher A]] |
| - | [[Category: Hartl, F U]] | + | [[Category: Hartl FU]] |
| - | [[Category: Hayer-Hartl, M]] | + | [[Category: Hayer-Hartl M]] |
| - | [[Category: Mueller-Cajar, O]] | + | [[Category: Mueller-Cajar O]] |
| - | [[Category: Stotz, M]] | + | [[Category: Stotz M]] |
| - | [[Category: Wendler, P]] | + | [[Category: Wendler P]] |
| - | [[Category: Aaa+ protein]]
| + | |
| - | [[Category: Calvin cycle]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Rubisco activase]]
| + | |
| Structural highlights
Function
CBBX_CERSP ATPase involved in the activation of red-type RuBisCo (ribulose-1,5-bisphosphate carboxylase/oxygenase), which tends to form inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP) (PubMed:22048315, PubMed:27872295). Catalyzes the release of RuBP from inhibited RuBisCo in an ATP-dependent manner (PubMed:22048315, PubMed:27872295). Activation of RuBisCO involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure (PubMed:22048315, PubMed:27872295).[1] [2]
Publication Abstract from PubMed
Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the fixation of atmospheric CO(2) in photosynthesis, but tends to form inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP). In plants, Rubisco is reactivated by the AAA(+) (ATPases associated with various cellular activities) protein Rubisco activase (Rca), but no such protein is known for the Rubisco of red algae. Here we identify the protein CbbX as an activase of red-type Rubisco. The 3.0-A crystal structure of unassembled CbbX from Rhodobacter sphaeroides revealed an AAA(+) protein architecture. Electron microscopy and biochemical analysis showed that ATP and RuBP must bind to convert CbbX into functionally active, hexameric rings. The CbbX ATPase is strongly stimulated by RuBP and Rubisco. Mutational analysis suggests that CbbX functions by transiently pulling the carboxy-terminal peptide of the Rubisco large subunit into the hexamer pore, resulting in the release of the inhibitory RuBP. Understanding Rubisco activation may facilitate efforts to improve CO(2) uptake and biomass production by photosynthetic organisms.
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase.,Mueller-Cajar O, Stotz M, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M Nature. 2011 Nov 2;479(7372):194-9. doi: 10.1038/nature10568. PMID:22048315[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mueller-Cajar O, Stotz M, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Nature. 2011 Nov 2;479(7372):194-9. doi: 10.1038/nature10568. PMID:22048315 doi:10.1038/nature10568
- ↑ Loganathan N, Tsai YC, Mueller-Cajar O. Characterization of the heterooligomeric red-type rubisco activase from red algae. Proc Natl Acad Sci U S A. 2016 Dec 6;113(49):14019-14024. PMID:27872295 doi:10.1073/pnas.1610758113
- ↑ Mueller-Cajar O, Stotz M, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Nature. 2011 Nov 2;479(7372):194-9. doi: 10.1038/nature10568. PMID:22048315 doi:10.1038/nature10568
|
