6jy5 | pdb_00006jy5
From Proteopedia
Structure of CsoS4B from Halothiobacillus neapolitanus
| ||||||||||||
Structural highlights
Publication Abstract from PubMedCarboxysome, 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 alpha-carboxysome possesses two 38% sequence-identical pentameric proteins, namely CsoS4A and CsoS4B. However, the functions of two paralogous pentameric proteins in alpha-carboxysome assembly remain unknown. Here we report the crystal structure of CsoS4B at 2.15A resolution. It displays as a stable pentamer, each subunit of which consists of a beta-barrel core domain, in addition to an insertion of helix alpha1 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 alpha-carboxysome, despite they share a similar overall structure. These findings provide the structural basis for further investigations on the self-assembly process of carboxysome. Crystal structure of pentameric shell protein CsoS4B of Halothiobacillus neapolitanus alpha-carboxysome.,Zhao YY, Jiang YL, Chen Y, Zhou CZ, Li Q Biochem Biophys Res Commun. 2019 Jul 30;515(3):510-515. doi:, 10.1016/j.bbrc.2019.05.047. Epub 2019 Jun 3. PMID:31171360[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||
This page was last modified 06:54, 26 June 2019.