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Crystal structure of pentameric shell protein CsoS4B of Halothiobacillus neapolitanus α-carboxysome
- Source :
- Biochemical and biophysical research communications. 515(3)
- Publication Year :
- 2019
-
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 A 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.
- Subjects :
- 0301 basic medicine
Models, Molecular
Pentamer
Pentameric protein
Protein subunit
Static Electricity
Biophysics
Shell (structure)
Crystal structure
Crystallography, X-Ray
Biochemistry
Halothiobacillus neapolitanus
03 medical and health sciences
0302 clinical medicine
Bacterial Proteins
Amino Acid Sequence
Molecular Biology
Chemistry
Cell Biology
Halothiobacillus
Carboxysome
030104 developmental biology
Structural Homology, Protein
030220 oncology & carcinogenesis
Helix
Protein Multimerization
Subjects
Details
- ISSN :
- 10902104
- Volume :
- 515
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....96f909ac014a4fae01971a0488283e15