Structural Characterization of a Newly Identified Component of α-Carboxysomes: The AAA+ Domain Protein CsoCbbQ

Sutter, Markus; Roberts, Evan W.; Gonzalez, Raul C.; Bates, Cassandra; Dawoud, Salma; Landry, Kimberly; Cannon, Gordon C.; Heinhorst, Sabine; Kerfeld, Cheryl A.

doi:10.1038/srep16243

Title: Structural Characterization of a Newly Identified Component of α-Carboxysomes: The AAA+ Domain Protein CsoCbbQ

Journal Article · Thu Nov 05 00:00:00 EST 2015 · Scientific Reports

DOI:https://doi.org/10.1038/srep16243· OSTI ID:1256062

Sutter, Markus ^[1]; Roberts, Evan W. ^[2]; Gonzalez, Raul C. ^[3]; Bates, Cassandra ^[2]; Dawoud, Salma ^[2]; Landry, Kimberly ^[2]; Cannon, Gordon C. ^[2]; Heinhorst, Sabine ^[2]; Kerfeld, Cheryl A. ^[4]

Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Univ. of Southern Mississippi, Hattiesburg, MS (United States)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Univ. of California, Berkeley, CA (United States); Michigan State Univ., East Lansing, MI (United States). Dept. of Biochemistry and Molecular Biology

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 α-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 α-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. Finally, 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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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Foundation (NSF)

Grant/Contract Number:: FG02-91ER20021; AC02-05CH11231; MCB-1244534

OSTI ID:: 1256062

Alternate ID(s):: OSTI ID: 1415945

Journal Information:: Scientific Reports, Vol. 5; ISSN 2045-2322

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 34 works

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