Structural highlights
Function
BMCH_HALO1 The only hexameric shell protein in this bacterium, it forms the majority of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms a 40 nm artificial BMC with a molecular mass of 6.5 MDa. There are 60 BMC-H hexamers per BMC. The shell facets are 20-30 Angstroms thick (a single hexamer layer), with 1 of BMC-T trimers protruding to the exterior.[1] [2]
References
- ↑ Sutter M, Greber B, Aussignargues C, Kerfeld CA. Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell. Science. 2017 Jun 23;356(6344):1293-1297. doi: 10.1126/science.aan3289. PMID:28642439 doi:http://dx.doi.org/10.1126/science.aan3289
- ↑ Greber BJ, Sutter M, Kerfeld CA. The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly. Structure. 2019 Feb 12. pii: S0969-2126(19)30017-6. doi:, 10.1016/j.str.2019.01.017. PMID:30833088 doi:http://dx.doi.org/10.1016/j.str.2019.01.017
