4ox6

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Revision as of 12:30, 1 February 2023

Structure of Synechococcus elongatus PCC 7942 CcmK4

Structural highlights

4ox6 is a 2 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.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCMK4_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] A minor shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered (Probable). Hexamers form sheets that form the facets of the polyhedral carboxysome. The shell is 4.5 nm thick, as observed for CcmK proteins (PubMed:28616951). In PCC 7942 there are several CcmK paralogs with presumably functional differences; replacing the central pore residues (34-37) with those of CcmK2 from this organism (Tyr-Glu-Lys-Ile) allows the bacterium to make carboxysomes, but the expression level is too low to know if the carboxysome is functional for CO(2) fixation (Probable). This subunit probably makes both homohexamers and heterohexamers with CcmK3. The CcmK3-CcmK4 heterohexmers have been suggested to cap other hexamers, perhaps to alter metabolite flux (Probable).^[1] ^[2] ^[3] ^[4]

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^[5]

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

References

↑ 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
↑ 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
↑ 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
↑ Sommer M, Sutter M, Gupta S, Kirst H, Turmo A, Lechno-Yossef S, Burton RL, Saechao C, Sloan NB, Cheng X, Chan LG, Petzold CJ, Fuentes-Cabrera M, Ralston CY, Kerfeld CA. Heterohexamers Formed by CcmK3 and CcmK4 Increase the Complexity of Beta Carboxysome Shells. Plant Physiol. 2019 Jan;179(1):156-167. doi: 10.1104/pp.18.01190. Epub 2018 Nov, 2. PMID:30389783 doi:http://dx.doi.org/10.1104/pp.18.01190
↑ 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/4ox6"

@@ Line 3: / Line 3: @@
 <StructureSection load='4ox6' size='340' side='right'caption='[[4ox6]], [[Resolution|resolution]] 1.34&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ox6]] is a 2 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=4OX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OX6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ox6]] is a 2 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=4OX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OX6 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Synpcc7942_0285 ([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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ox6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ox6 OCA], [https://pdbe.org/4ox6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ox6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ox6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ox6 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=4ox6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ox6 OCA], [http://pdbe.org/4ox6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ox6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ox6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ox6 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CCMK4_SYNE7 CCMK4_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]  A minor shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered (Probable). Hexamers form sheets that form the facets of the polyhedral carboxysome. The shell is 4.5 nm thick, as observed for CcmK proteins (PubMed:28616951). In PCC 7942 there are several CcmK paralogs with presumably functional differences; replacing the central pore residues (34-37) with those of CcmK2 from this organism (Tyr-Glu-Lys-Ile) allows the bacterium to make carboxysomes, but the expression level is too low to know if the carboxysome is functional for CO(2) fixation (Probable). This subunit probably makes both homohexamers and heterohexamers with CcmK3. The CcmK3-CcmK4 heterohexmers have been suggested to cap other hexamers, perhaps to alter metabolite flux (Probable).<ref>PMID:28616951</ref> <ref>PMID:22928045</ref> <ref>PMID:25117559</ref> <ref>PMID:30389783</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 21: @@
 __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]]

4ox6

From Proteopedia

Revision as of 12:30, 1 February 2023

Structure of Synechococcus elongatus PCC 7942 CcmK4

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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