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| | <StructureSection load='6uew' size='340' side='right'caption='[[6uew]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='6uew' size='340' side='right'caption='[[6uew]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6uew]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Halnc Halnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UEW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6uew]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Halothiobacillus_neapolitanus_c2 Halothiobacillus neapolitanus c2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UEW FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbbL, Hneap_0922 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=555778 HALNC]), cbbS, rbcS, Hneap_0921 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=555778 HALNC])</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]] 2.4Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </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=6uew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uew OCA], [https://pdbe.org/6uew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uew RCSB], [https://www.ebi.ac.uk/pdbsum/6uew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uew ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6uew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uew OCA], [http://pdbe.org/6uew PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uew RCSB], [http://www.ebi.ac.uk/pdbsum/6uew PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uew ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RBL1_HALNC RBL1_HALNC]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] [[http://www.uniprot.org/uniprot/RBS_HALNC RBS_HALNC]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. | + | [https://www.uniprot.org/uniprot/RBL1_HALNC RBL1_HALNC] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Halnc]] | + | [[Category: Halothiobacillus neapolitanus c2]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribulose-bisphosphate carboxylase]]
| + | [[Category: Oltrogge LM]] |
| - | [[Category: Oltrogge, L M]] | + | [[Category: Savage DF]] |
| - | [[Category: Savage, D F]] | + | |
| - | [[Category: Carboxysome]]
| + | |
| - | [[Category: Csos2]]
| + | |
| - | [[Category: Phase separation]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Rubisco]]
| + | |
| Structural highlights
Function
RBL1_HALNC RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
Publication Abstract from PubMed
Carboxysomes are bacterial microcompartments that function as the centerpiece of the bacterial CO2-concentrating mechanism by facilitating high CO2 concentrations near the carboxylase Rubisco. The carboxysome self-assembles from thousands of individual proteins into icosahedral-like particles with a dense enzyme cargo encapsulated within a proteinaceous shell. In the case of the alpha-carboxysome, there is little molecular insight into protein-protein interactions that drive the assembly process. Here, studies on the alpha-carboxysome from Halothiobacillus neapolitanus demonstrate that Rubisco interacts with the N terminus of CsoS2, a multivalent, intrinsically disordered protein. X-ray structural analysis of the CsoS2 interaction motif bound to Rubisco reveals a series of conserved electrostatic interactions that are only made with properly assembled hexadecameric Rubisco. Although biophysical measurements indicate that this single interaction is weak, its implicit multivalency induces high-affinity binding through avidity. Taken together, our results indicate that CsoS2 acts as an interaction hub to condense Rubisco and enable efficient alpha-carboxysome formation.
Multivalent interactions between CsoS2 and Rubisco mediate alpha-carboxysome formation.,Oltrogge LM, Chaijarasphong T, Chen AW, Bolin ER, Marqusee S, Savage DF Nat Struct Mol Biol. 2020 Mar;27(3):281-287. doi: 10.1038/s41594-020-0387-7. Epub, 2020 Mar 2. PMID:32123388[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oltrogge LM, Chaijarasphong T, Chen AW, Bolin ER, Marqusee S, Savage DF. Multivalent interactions between CsoS2 and Rubisco mediate alpha-carboxysome formation. Nat Struct Mol Biol. 2020 Mar;27(3):281-287. doi: 10.1038/s41594-020-0387-7. Epub, 2020 Mar 2. PMID:32123388 doi:http://dx.doi.org/10.1038/s41594-020-0387-7
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