2EWH

Carboxysome protein CsoS1A from Halothiobacillus neapolitanus

2EWH の概要

• エントリーDOI: 10.2210/pdb2ewh/pdb
• 分子名称: Major carboxysome shell protein 1A, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: bacterial microcompartment domain, carboxysome
• 由来する生物種: Halothiobacillus neapolitanus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10157.69

構造登録者

Tsai, Y.,Sawaya, M.R.,Kerfeld, C.A.,Yeates, T.O. (登録日: 2005-11-03, 公開日: 2006-11-14, 最終更新日: 2023-08-23)

主引用文献

Tsai, Y.,Sawaya, M.R.,Cannon, G.C.,Cai, F.,Williams, E.B.,Heinhorst, S.,Kerfeld, C.A.,Yeates, T.O.
Structural Analysis of CsoS1A and the Protein Shell of the Halothiobacillus neapolitanus Carboxysome.
Plos Biol., 5:e144-, 2007

PubMed Abstract: The carboxysome is a bacterial organelle that functions to enhance the efficiency of CO2 fixation by encapsulating the enzymes ribulose bisphosphate carboxylase/oxygenase (RuBisCO) and carbonic anhydrase. The outer shell of the carboxysome is reminiscent of a viral capsid, being constructed from many copies of a few small proteins. Here we describe the structure of the shell protein CsoS1A from the chemoautotrophic bacterium Halothiobacillus neapolitanus. The CsoS1A protein forms hexameric units that pack tightly together to form a molecular layer, which is perforated by narrow pores. Sulfate ions, soaked into crystals of CsoS1A, are observed in the pores of the molecular layer, supporting the idea that the pores could be the conduit for negatively charged metabolites such as bicarbonate, which must cross the shell. The problem of diffusion across a semiporous protein shell is discussed, with the conclusion that the shell is sufficiently porous to allow adequate transport of small molecules. The molecular layer formed by CsoS1A is similar to the recently observed layers formed by cyanobacterial carboxysome shell proteins. This similarity supports the argument that the layers observed represent the natural structure of the facets of the carboxysome shell. Insights into carboxysome function are provided by comparisons of the carboxysome shell to viral capsids, and a comparison of its pores to the pores of transmembrane protein channels.

PubMed: 17518518
DOI: 10.1371/journal.pbio.0050144

実験手法

X-RAY DIFFRACTION (1.4 Å)