5C3C

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

5C3C の概要

• エントリーDOI: 10.2210/pdb5c3c/pdb
• 分子名称: CbbQ/NirQ/NorQ domain protein, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: atpase, aaa+ domain protein, carboxysome-associated, protein binding
• 由来する生物種: Halothiobacillus neapolitanus (strain ATCC 23641 / c2)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64344.85

構造登録者

Sutter, M.,Kerfeld, C.A. (登録日: 2015-06-17, 公開日: 2015-11-18, 最終更新日: 2024-03-06)

主引用文献

Sutter, M.,Roberts, E.W.,Gonzalez, R.C.,Bates, C.,Dawoud, S.,Landry, K.,Cannon, G.C.,Heinhorst, S.,Kerfeld, C.A.
Structural Characterization of a Newly Identified Component of alpha-Carboxysomes: The AAA+ Domain Protein CsoCbbQ.
Sci Rep, 5:16243-16243, 2015

PubMed Abstract: 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. 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.

PubMed: 26538283
DOI: 10.1038/srep16243

実験手法

X-RAY DIFFRACTION (2.8 Å)