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Crystal structure of pentameric shell protein CsoS4B of Halothiobacillus neapolitanus α-carboxysome.

Abstract：

:Carboxysome, encapsulating an enzymatic core within an icosahedral-shaped semipermeable protein shell, could enhance CO2 fixation under low CO2 conditions in the environment. The shell of Halothiobacillus neapolitanus α-carboxysome possesses two 38% sequence-identical pentameric proteins, namely CsoS4A and CsoS4B. However, the functions of two paralogous pentameric proteins in α-carboxysome assembly remain unknown. Here we report the crystal structure of CsoS4B at 2.15 Å resolution. It displays as a stable pentamer, each subunit of which consists of a β-barrel core domain, in addition to an insertion of helix α1 that forms the central pore. Structural comparisons and multiple-sequence alignment strongly indicate that CsoS4A and CsoS4B differ from each other in interacting with various components of α-carboxysome, despite they share a similar overall structure. These findings provide the structural basis for further investigations on the self-assembly process of carboxysome.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Zhao YY,Jiang YL,Chen Y,Zhou CZ,Li Q

doi

10.1016/j.bbrc.2019.05.047

subject

Has Abstract

pub_date

2019-07-30 00:00:00

pages

510-515

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(19)30915-5

journal_volume

515

pub_type

杂志文章

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