4ht5: Difference between revisions
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== | ==CO2 concentrating mechanism protein P, CcmP form 1== | ||
[[4ht5]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <StructureSection load='4ht5' size='340' side='right' caption='[[4ht5]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ht5]] is a 6 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=4HT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HT5 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ht7|4ht7]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ht5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ht5 OCA], [http://pdbe.org/4ht5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ht5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ht5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ht5 ProSAT]</span></td></tr> | |||
</table> | |||
<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> | |||
<ref | |||
[[Category: | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: Cai, F | </div> | ||
[[Category: Kerfeld, C A | <div class="pdbe-citations 4ht5" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Anacystis nidulans]] | |||
[[Category: Cai, F]] | |||
[[Category: Kerfeld, C A]] | |||
[[Category: Sutter, M]] | [[Category: Sutter, M]] | ||
[[Category: Bmc]] | [[Category: Bmc]] | ||
[[Category: Carboxysome]] | [[Category: Carboxysome]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
Revision as of 07:18, 4 August 2016
CO2 concentrating mechanism protein P, CcmP form 1
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