4ox7

From Proteopedia

(Difference between revisions)

Current revision

Structure of Synechococcus elongatus PCC 7942 CcmK2

Structural highlights

4ox7 is a 6 chain structure with sequence from Synechococcus elongatus PCC 7942 = FACHB-805. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1001Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCMK2_SYNE7 One of the shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome. The hexamer central pore probably regulates metabolite flux.[HAMAP-Rule:MF_00854] The major shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Hexamers make sheets that form the facets of the polyhedral carboxysome (PubMed:22928045). The shell is 4.5 nm thick, as observed for CcmK hexamers (PubMed:28616951). Required for recruitment of CcmO to the pre-carboxysome (PubMed:22928045, PubMed:24267892). In PCC 7942 there are several CcmK paralogs with presumably functional differences; replacing the central pore residues (34-37) with those of either CcmK4 from this organism (Tyr-Met-Arg-Ala) or from an alpha-type carboxysome forming cyanobacterium (CsoS1 of P.marinus strain MIT 9313, Arg-Glu-Phe-Val) allows the bacterium to make carboxysomes, but the expression level is too low to know if the carboxysome is functional for CO(2) fixation (PubMed:25117559).^[1] ^[2] ^[3] ^[4] 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 CcmM58 and CcmM35. CcmN interacts with the N-terminus of CcmM58, and then recruits the CcmK2 major shell protein via CcmN's encapsulation peptide. Shell formation requires 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.^[5]

Publication Abstract from PubMed

Bacterial microcompartments (BMCs) are self-assembling organelles composed entirely of protein. Depending on the enzymes they encapsulate, BMCs function in either inorganic carbon fixation (carboxysomes) or organic carbon utilization (metabolosomes). The hallmark feature of all BMCs is a selectively permeable shell formed by multiple paralogous proteins, each proposed to confer specific flux characteristics. Gene clusters encoding diverse BMCs are distributed broadly across bacterial phyla, providing a rich variety of building blocks with a predicted range of permeability properties. In theory, shell permeability can be engineered by modifying residues flanking the pores (symmetry axes) of hexameric shell proteins or by combining shell proteins from different types of BMCs into chimeric shells. We undertook both approaches to altering shell properties using the carboxysome as a model system. There are two types of carboxysomes, alpha and beta. In both, the predominant shell protein(s) contain a single copy of the BMC domain (pfam00936), but they are significantly different in primary structure. Indeed, phylogenetic analysis shows that the two types of carboxysome shell proteins are more similar to their counterparts in metabolosomes than to each other. We solved high resolution crystal structures of the major shell proteins, CsoS1 and CcmK2 and the presumed minor shell protein CcmK4, representing both types of cyanobacterial carboxysomes and then tested the interchangeability. The in vivo study presented here confirms that both engineering pores to mimic those of other shell proteins and the construction of chimeric shells is feasible.

Engineering Bacterial Microcompartment Shells: Chimeric Shell Proteins and Chimeric Carboxysome Shells.,Cai F, Sutter M, Bernstein SL, Kinney JN, Kerfeld CA ACS Synth Biol. 2014 Aug 12. PMID:25117559^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rae BD, Long BM, Badger MR, Price GD. Structural determinants of the outer shell of beta-carboxysomes in Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL. PLoS One. 2012;7(8):e43871. doi: 10.1371/journal.pone.0043871. Epub 2012 Aug 22. PMID:22928045 doi:http://dx.doi.org/10.1371/journal.pone.0043871
↑ Cameron JC, Wilson SC, Bernstein SL, Kerfeld CA. Biogenesis of a bacterial organelle: the carboxysome assembly pathway. Cell. 2013 Nov 21;155(5):1131-40. doi: 10.1016/j.cell.2013.10.044. PMID:24267892 doi:http://dx.doi.org/10.1016/j.cell.2013.10.044
↑ Cai F, Sutter M, Bernstein SL, Kinney JN, Kerfeld CA. Engineering Bacterial Microcompartment Shells: Chimeric Shell Proteins and Chimeric Carboxysome Shells. ACS Synth Biol. 2014 Aug 12. PMID:25117559 doi:http://dx.doi.org/10.1021/sb500226j
↑ Faulkner M, Rodriguez-Ramos J, Dykes GF, Owen SV, Casella S, Simpson DM, Beynon RJ, Liu LN. Direct characterization of the native structure and mechanics of cyanobacterial carboxysomes. Nanoscale. 2017 Aug 3;9(30):10662-10673. doi: 10.1039/c7nr02524f. PMID:28616951 doi:http://dx.doi.org/10.1039/c7nr02524f
↑ Cameron JC, Wilson SC, Bernstein SL, Kerfeld CA. Biogenesis of a bacterial organelle: the carboxysome assembly pathway. Cell. 2013 Nov 21;155(5):1131-40. doi: 10.1016/j.cell.2013.10.044. PMID:24267892 doi:http://dx.doi.org/10.1016/j.cell.2013.10.044
↑ Cai F, Sutter M, Bernstein SL, Kinney JN, Kerfeld CA. Engineering Bacterial Microcompartment Shells: Chimeric Shell Proteins and Chimeric Carboxysome Shells. ACS Synth Biol. 2014 Aug 12. PMID:25117559 doi:http://dx.doi.org/10.1021/sb500226j

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ox7"

@@ Line 3: / Line 3: @@
 <StructureSection load='4ox7' size='340' side='right'caption='[[4ox7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ox7]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OX7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ox7]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OX7 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Synpcc7942_1421,ccmK,csoS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Anacystis nidulans R2])</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]] 2.1001&#8491;</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=4ox7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ox7 OCA], [http://pdbe.org/4ox7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ox7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ox7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ox7 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=4ox7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ox7 OCA], [https://pdbe.org/4ox7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ox7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ox7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ox7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CCMK_SYNE7 CCMK_SYNE7]] May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered.
+[https://www.uniprot.org/uniprot/CCMK2_SYNE7 CCMK2_SYNE7] One of the shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome. The hexamer central pore probably regulates metabolite flux.[HAMAP-Rule:MF_00854]  The major shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Hexamers make sheets that form the facets of the polyhedral carboxysome (PubMed:22928045). The shell is 4.5 nm thick, as observed for CcmK hexamers (PubMed:28616951). Required for recruitment of CcmO to the pre-carboxysome (PubMed:22928045, PubMed:24267892). In PCC 7942 there are several CcmK paralogs with presumably functional differences; replacing the central pore residues (34-37) with those of either CcmK4 from this organism (Tyr-Met-Arg-Ala) or from an alpha-type carboxysome forming cyanobacterium (CsoS1 of P.marinus strain MIT 9313, Arg-Glu-Phe-Val) allows the bacterium to make carboxysomes, but the expression level is too low to know if the carboxysome is functional for CO(2) fixation (PubMed:25117559).<ref>PMID:22928045</ref> <ref>PMID:24267892</ref> <ref>PMID:25117559</ref> <ref>PMID:28616951</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 CcmM58 and CcmM35. CcmN interacts with the N-terminus of CcmM58, and then recruits the CcmK2 major shell protein via CcmN's encapsulation peptide. Shell formation requires 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.<ref>PMID:24267892</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Anacystis nidulans r2]]
 [[Category: Large Structures]]
-[[Category: Cai, F]]
+[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
-[[Category: Kerfeld, C A]]
+[[Category: Cai F]]
-[[Category: Kinney, J N]]
+[[Category: Kerfeld CA]]
-[[Category: Sutter, M]]
+[[Category: Kinney JN]]
-[[Category: Bacterial microcompartment]]
+[[Category: Sutter M]]
-[[Category: Structural protein]]

4ox7

From Proteopedia

Current revision

Structure of Synechococcus elongatus PCC 7942 CcmK2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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