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| | <StructureSection load='2rcf' size='340' side='right'caption='[[2rcf]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='2rcf' size='340' side='right'caption='[[2rcf]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rcf]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/"thiobacillus_x"_parker_and_prisk_1953 "thiobacillus x" parker and prisk 1953]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RCF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rcf]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Halothiobacillus_neapolitanus Halothiobacillus neapolitanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RCF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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]] 2.15Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORFA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=927 "Thiobacillus X" Parker and Prisk 1953])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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=2rcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcf OCA], [https://pdbe.org/2rcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rcf RCSB], [https://www.ebi.ac.uk/pdbsum/2rcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rcf 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=2rcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcf OCA], [https://pdbe.org/2rcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rcf RCSB], [https://www.ebi.ac.uk/pdbsum/2rcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rcf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CSS4A_HALNC CSS4A_HALNC] Probably forms vertices in the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered. Has been modeled to induce curvature upon insertion into an otherwise flat hexagonal layer of major carboxysome subunits (Probable). A minor shell protein, only 12 pentamers of CsoS4A/CsoS4B are calculated to be present in each carboxysome. The 2 CsoS4 proteins contribute to the impermeability of the carboxysome to CO(2) (PubMed:19844578).<ref>PMID:19844578</ref> <ref>PMID:18292340</ref> Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell.<ref>PMID:33116131</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thiobacillus x parker and prisk 1953]] | + | [[Category: Halothiobacillus neapolitanus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kerfeld, C A]] | + | [[Category: Kerfeld CA]] |
| - | [[Category: Sawaya, M R]] | + | [[Category: Sawaya MR]] |
| - | [[Category: Yeates, T O]] | + | [[Category: Yeates TO]] |
| - | [[Category: Cyclic pentamer]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
CSS4A_HALNC Probably forms vertices in the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered. Has been modeled to induce curvature upon insertion into an otherwise flat hexagonal layer of major carboxysome subunits (Probable). A minor shell protein, only 12 pentamers of CsoS4A/CsoS4B are calculated to be present in each carboxysome. The 2 CsoS4 proteins contribute to the impermeability of the carboxysome to CO(2) (PubMed:19844578).[1] [2] Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell.[3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The carboxysome is a bacterial microcompartment that functions as a simple organelle by sequestering enzymes involved in carbon fixation. The carboxysome shell is roughly 800 to 1400 angstroms in diameter and is assembled from several thousand protein subunits. Previous studies have revealed the three-dimensional structures of hexameric carboxysome shell proteins, which self-assemble into molecular layers that most likely constitute the facets of the polyhedral shell. Here, we report the three-dimensional structures of two proteins of previously unknown function, CcmL and OrfA (or CsoS4A), from the two known classes of carboxysomes, at resolutions of 2.4 and 2.15 angstroms. Both proteins assemble to form pentameric structures whose size and shape are compatible with formation of vertices in an icosahedral shell. Combining these pentamers with the hexamers previously elucidated gives two plausible, preliminary atomic models for the carboxysome shell.
Atomic-level models of the bacterial carboxysome shell.,Tanaka S, Kerfeld CA, Sawaya MR, Cai F, Heinhorst S, Cannon GC, Yeates TO Science. 2008 Feb 22;319(5866):1083-6. PMID:18292340[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cai F, Menon BB, Cannon GC, Curry KJ, Shively JM, Heinhorst S. The pentameric vertex proteins are necessary for the icosahedral carboxysome shell to function as a CO2 leakage barrier. PLoS One. 2009 Oct 21;4(10):e7521. PMID:19844578 doi:10.1371/journal.pone.0007521
- ↑ Tanaka S, Kerfeld CA, Sawaya MR, Cai F, Heinhorst S, Cannon GC, Yeates TO. Atomic-level models of the bacterial carboxysome shell. Science. 2008 Feb 22;319(5866):1083-6. PMID:18292340 doi:http://dx.doi.org/319/5866/1083
- ↑ Li T, Jiang Q, Huang J, Aitchison CM, Huang F, Yang M, Dykes GF, He HL, Wang Q, Sprick RS, Cooper AI, Liu LN. Reprogramming bacterial protein organelles as a nanoreactor for hydrogen production. Nat Commun. 2020 Oct 28;11(1):5448. doi: 10.1038/s41467-020-19280-0. PMID:33116131 doi:http://dx.doi.org/10.1038/s41467-020-19280-0
- ↑ Tanaka S, Kerfeld CA, Sawaya MR, Cai F, Heinhorst S, Cannon GC, Yeates TO. Atomic-level models of the bacterial carboxysome shell. Science. 2008 Feb 22;319(5866):1083-6. PMID:18292340 doi:http://dx.doi.org/319/5866/1083
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