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| | ==CO2 concentrating mechanism protein P, CcmP form 2== | | ==CO2 concentrating mechanism protein P, CcmP form 2== |
| - | <StructureSection load='4ht7' size='340' side='right' caption='[[4ht7]], [[Resolution|resolution]] 3.30Å' scene=''> | + | <StructureSection load='4ht7' size='340' side='right'caption='[[4ht7]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ht7]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HT7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HT7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ht7]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_6301 Synechococcus elongatus PCC 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HT7 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ht5|4ht5]]</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]] 3.301Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">syc1000_c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269084 Anacystis nidulans])</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=4ht7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ht7 OCA], [https://pdbe.org/4ht7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ht7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ht7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ht7 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=4ht7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ht7 OCA], [http://pdbe.org/4ht7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ht7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ht7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ht7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/CCMP_SYNE7 CCMP_SYNE7] Probably part of the carboxysome shell, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. It is thought that this protein controls transport of RuBisCO reactants in and out of the carboxysome; residual densities in the 4 X-ray structures suggest that differing compounds bind in interior pockets, depending on the open or closed state of the pore.<ref>PMID:23572529</ref> |
| - | The carboxysome is a bacterial organelle found in all cyanobacteria; it encapsulates CO2 fixation enzymes within a protein shell. The most abundant carboxysome shell protein contains a single bacterial microcompartment (BMC) domain. We present in vivo evidence that a hypothetical protein (dubbed CcmP) encoded in all beta-cyanobacterial genomes is part of the carboxysome. We show that CcmP is a tandem BMC domain protein, the first to be structurally characterized from a beta-carboxysome. CcmP forms a dimer of tightly stacked trimers, resulting in a nanocompartment-containing shell protein that may weakly bind 3-phosphoglycerate, the product of CO2 fixation. The trimers have a large central pore through which metabolites presumably pass into the carboxysome. Conserved residues surrounding the pore have alternate side-chain conformations suggesting that it can be open or closed. Furthermore, CcmP and its orthologs in alpha-cyanobacterial genomes form a distinct clade of shell proteins. Members of this subgroup are also found in numerous heterotrophic BMC-associated gene clusters encoding functionally diverse bacterial organelles, suggesting that the potential to form a nanocompartment within a microcompartment shell is widespread. Given that carboxysomes and architecturally related bacterial organelles are the subject of intense interest for applications in synthetic biology/metabolic engineering, our results describe a new type of building block with which to functionalize BMC shells.
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| - | The structure of CcmP, a tandem bacterial microcompartment domain protein from the beta-carboxysome, forms a subcompartment within a microcompartment.,Cai F, Sutter M, Cameron JC, Stanley DN, Kinney JN, Kerfeld CA J Biol Chem. 2013 May 31;288(22):16055-63. doi: 10.1074/jbc.M113.456897. Epub, 2013 Apr 9. PMID:23572529<ref>PMID:23572529</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 4ht7" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anacystis nidulans]] | + | [[Category: Large Structures]] |
| - | [[Category: Cai, F]] | + | [[Category: Synechococcus elongatus PCC 6301]] |
| - | [[Category: Kerfeld, C A]] | + | [[Category: Cai F]] |
| - | [[Category: Sutter, M]] | + | [[Category: Kerfeld CA]] |
| - | [[Category: Bmc]] | + | [[Category: Sutter M]] |
| - | [[Category: Carboxysome]]
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| - | [[Category: Protein binding]]
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