5c3c

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==Structural characterization of a newly identified component of alpha-carboxysomes: The AAA+ domain Protein cso-CbbQ==
==Structural characterization of a newly identified component of alpha-carboxysomes: The AAA+ domain Protein cso-CbbQ==
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<StructureSection load='5c3c' size='340' side='right' caption='[[5c3c]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='5c3c' size='340' side='right'caption='[[5c3c]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5c3c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C3C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5c3c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Halothiobacillus_neapolitanus_c2 Halothiobacillus neapolitanus c2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C3C FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<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=5c3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c3c OCA], [http://pdbe.org/5c3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c3c RCSB], [http://www.ebi.ac.uk/pdbsum/5c3c PDBsum]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5c3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c3c OCA], [https://pdbe.org/5c3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c3c RCSB], [https://www.ebi.ac.uk/pdbsum/5c3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c3c ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/D0KZ75_HALNC D0KZ75_HALNC]
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Carboxysomes are bacterial microcompartments that enhance carbon fixation by concentrating ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and its substrate CO2 within a proteinaceous shell. They are found in all cyanobacteria, some purple photoautotrophs and many chemoautotrophic bacteria. Carboxysomes consist of a protein shell that encapsulates several hundred molecules of RuBisCO, and contain carbonic anhydrase and other accessory proteins. Genes coding for carboxysome shell components and the encapsulated proteins are typically found together in an operon. The alpha-carboxysome operon is embedded in a cluster of additional, conserved genes that are presumably related to its function. In many chemoautotrophs, products of the expanded carboxysome locus include CbbO and CbbQ, a member of the AAA+ domain superfamily. We bioinformatically identified subtypes of CbbQ proteins and show that their genes frequently co-occur with both Form IA and Form II RuBisCO. The alpha-carboxysome-associated ortholog, CsoCbbQ, from Halothiobacillus neapolitanus forms a hexamer in solution and hydrolyzes ATP. The crystal structure shows that CsoCbbQ is a hexamer of the typical AAA+ domain; the additional C-terminal domain, diagnostic of the CbbQ subfamily, structurally fills the inter-monomer gaps, resulting in a distinctly hexagonal shape. We show that CsoCbbQ interacts with CsoCbbO and is a component of the carboxysome shell, the first example of ATPase activity associated with a bacterial microcompartment.
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Structural Characterization of a Newly Identified Component of alpha-Carboxysomes: The AAA+ Domain Protein CsoCbbQ.,Sutter M, Roberts EW, Gonzalez RC, Bates C, Dawoud S, Landry K, Cannon GC, Heinhorst S, Kerfeld CA Sci Rep. 2015 Nov 5;5:16243. doi: 10.1038/srep16243. PMID:26538283<ref>PMID:26538283</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5c3c" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Kerfeld, C A]]
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[[Category: Halothiobacillus neapolitanus c2]]
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[[Category: Sutter, M]]
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[[Category: Large Structures]]
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[[Category: Aaa+ domain protein]]
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[[Category: Kerfeld CA]]
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[[Category: Atpase]]
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[[Category: Sutter M]]
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[[Category: Carboxysome-associated]]
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[[Category: Protein binding]]
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Current revision

Structural characterization of a newly identified component of alpha-carboxysomes: The AAA+ domain Protein cso-CbbQ

PDB ID 5c3c

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