4ht5: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ht5]] is a 6 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=4HT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HT5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ht5]] is a 6 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=4HT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HT5 FirstGlance]. <br>
</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=4ht5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ht5 OCA], [https://pdbe.org/4ht5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ht5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ht5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ht5 ProSAT]</span></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]] 2.51&#8491;</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=4ht5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ht5 OCA], [https://pdbe.org/4ht5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ht5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ht5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ht5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[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>  
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ht5" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 14:44, 1 March 2024

CO2 concentrating mechanism protein P, CcmP form 1CO2 concentrating mechanism protein P, CcmP form 1

Structural highlights

4ht5 is a 6 chain structure with sequence from Synechococcus elongatus PCC 6301. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.51Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

References

  1. ↑ Cai F, Sutter M, Cameron JC, Stanley DN, Kinney JN, Kerfeld CA. The structure of CcmP, a tandem bacterial microcompartment domain protein from the beta-carboxysome, forms a subcompartment within a microcompartment. J Biol Chem. 2013 May 31;288(22):16055-63. doi: 10.1074/jbc.M113.456897. Epub, 2013 Apr 9. PMID:23572529 doi:10.1074/jbc.M113.456897

4ht5, resolution 2.51Å

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