5c3c: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5c3c' size='340' side='right'caption='[[5c3c]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='5c3c' size='340' side='right'caption='[[5c3c]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5c3c]] is a 2 chain structure with sequence from [ | <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> | ||
</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><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> | ||
<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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D0KZ75_HALNC D0KZ75_HALNC] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Halothiobacillus neapolitanus c2]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kerfeld | [[Category: Kerfeld CA]] | ||
[[Category: Sutter | [[Category: Sutter M]] | ||
Revision as of 09:18, 7 June 2023
Structural characterization of a newly identified component of alpha-carboxysomes: The AAA+ domain Protein cso-CbbQStructural characterization of a newly identified component of alpha-carboxysomes: The AAA+ domain Protein cso-CbbQ
Structural highlights
FunctionPublication Abstract from PubMedCarboxysomes 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||