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| | <StructureSection load='6mr1' size='340' side='right'caption='[[6mr1]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='6mr1' size='340' side='right'caption='[[6mr1]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mr1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Theeb Theeb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MR1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mr1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus_BP-1 Thermosynechococcus vestitus BP-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MR1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene>, <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]] 1.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kwc|3kwc]]</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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ccmM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB])</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=6mr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mr1 OCA], [https://pdbe.org/6mr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mr1 RCSB], [https://www.ebi.ac.uk/pdbsum/6mr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mr1 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=6mr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mr1 OCA], [http://pdbe.org/6mr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mr1 RCSB], [http://www.ebi.ac.uk/pdbsum/6mr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mr1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/CCMM_THEVB CCMM_THEVB] Functions as a scaffold protein for the assembly of beta-carboxysomes, initiates carboxysome assembly by coalescing RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) (Probable). Produced as a full-length and a shorter form; both forms are required for correct carboxysome assembly and growth (By similarity).[UniProtKB:Q03513]<ref>PMID:30591587</ref> A carbonic anhydrase, catalyzes the reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation, supplies CO(2) to ribulose bisphosphate carboxylase (RuBisCO) in the carboxysome. Active when the disulfide bond (194-200) is oxidized, suggesting the interior of the carboxysome is oxidizing.<ref>PMID:20133749</ref> Beta-carboxysome assembly initiates when soluble RuBisCO is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both forms of CcmM (Probable). CcmN interacts with the N-terminus of full length CcmM, and then recruits the shell proteins (CcmK) via CcmN's encapsulation peptide. Shell formation requires both CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully encapsulated carboxysomes are formed, they migrate within the cell probably via interactions with the cytoskeleton (By similarity).[UniProtKB:Q03513]<ref>PMID:30591587</ref> |
| - | Carboxysomes are compartments in bacterial cells that promote efficient carbon fixation by sequestering RubisCO and carbonic anhydrase within a protein shell that impedes CO2 escape. The key to assembling this protein complex is CcmM, a multidomain protein whose C-terminal region is required for RubisCO recruitment. This CcmM region is built as a series of copies (generally 3-5) of a small domain, CcmMS, joined by unstructured linkers. CcmMS domains have weak, but significant, sequence identity to RubisCO's small subunit, RbcS, suggesting that CcmM binds RubisCO by displacing RbcS. We report here the 1.35 A structure of the first Thermosynechococcus elongatus CcmMS domain, revealing that it adopts a compact, well-defined structure that resembles that of RbcS. CcmMS, however, lacked key RbcS RubisCO-binding determinants, most notably an extended N-terminal loop. Nevertheless, individual CcmMS domains are able to bind RubisCO in vitro with 1.16 muM affinity. Two or four linked CcmMS domains did not exhibit dramatic increases in this affinity, implying that short, disordered linkers may frustrate successive CcmMS domains attempting to simultaneously bind a single RubisCO oligomer. Size-exclusion chromatography-coupled right-angled light scattering (SEC-RALS) and native MS experiments indicated that multiple CcmMS domains can bind a single RubisCO holoenzyme and, moreover, that RbcS is not released from these complexes. CcmMS bound equally tightly to a RubisCO variant in which the alpha/beta domain of RbcS was deleted, suggesting that CcmMS binds RubisCO independently of its RbcS subunit. We propose that, instead, the electropositive CcmMS may bind to an extended electronegative pocket between RbcL dimers.
| + | |
| - | | + | |
| - | The small RbcS-like domains of the beta-carboxysome structural protein, CcmM, bind RubisCO at a site distinct from that binding the RbcS subunit.,Ryan P, Forrester TJB, Wroblewski C, Kenney TMG, Kitova EN, Klassen JS, Kimber MS J Biol Chem. 2018 Dec 27. pii: RA118.006330. doi: 10.1074/jbc.RA118.006330. PMID:30591587<ref>PMID:30591587</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6mr1" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Theeb]] | + | [[Category: Thermosynechococcus vestitus BP-1]] |
| - | [[Category: Kimber, M S]] | + | [[Category: Kimber MS]] |
| - | [[Category: Ryan, P]] | + | [[Category: Ryan P]] |
| - | [[Category: Carboxysome]]
| + | |
| - | [[Category: Ccmm]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Rubisco]]
| + | |
| Structural highlights
Function
CCMM_THEVB Functions as a scaffold protein for the assembly of beta-carboxysomes, initiates carboxysome assembly by coalescing RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) (Probable). Produced as a full-length and a shorter form; both forms are required for correct carboxysome assembly and growth (By similarity).[UniProtKB:Q03513][1] A carbonic anhydrase, catalyzes the reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation, supplies CO(2) to ribulose bisphosphate carboxylase (RuBisCO) in the carboxysome. Active when the disulfide bond (194-200) is oxidized, suggesting the interior of the carboxysome is oxidizing.[2] Beta-carboxysome assembly initiates when soluble RuBisCO is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both forms of CcmM (Probable). CcmN interacts with the N-terminus of full length CcmM, and then recruits the shell proteins (CcmK) via CcmN's encapsulation peptide. Shell formation requires both CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully encapsulated carboxysomes are formed, they migrate within the cell probably via interactions with the cytoskeleton (By similarity).[UniProtKB:Q03513][3]
References
- ↑ Ryan P, Forrester TJB, Wroblewski C, Kenney TMG, Kitova EN, Klassen JS, Kimber MS. The small RbcS-like domains of the beta-carboxysome structural protein, CcmM, bind RubisCO at a site distinct from that binding the RbcS subunit. J Biol Chem. 2018 Dec 27. pii: RA118.006330. doi: 10.1074/jbc.RA118.006330. PMID:30591587 doi:http://dx.doi.org/10.1074/jbc.RA118.006330
- ↑ Pena KL, Castel SE, de Araujo C, Espie GS, Kimber MS. Structural basis of the oxidative activation of the carboxysomal gamma-carbonic anhydrase, CcmM. Proc Natl Acad Sci U S A. 2010 Feb 9;107(6):2455-60. Epub 2010 Jan 25. PMID:20133749
- ↑ Ryan P, Forrester TJB, Wroblewski C, Kenney TMG, Kitova EN, Klassen JS, Kimber MS. The small RbcS-like domains of the beta-carboxysome structural protein, CcmM, bind RubisCO at a site distinct from that binding the RbcS subunit. J Biol Chem. 2018 Dec 27. pii: RA118.006330. doi: 10.1074/jbc.RA118.006330. PMID:30591587 doi:http://dx.doi.org/10.1074/jbc.RA118.006330
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