Structural highlights
Function
BMCT2_HALO1 A minor component 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 40 nm artificial BMCs with a molecular mass of 6.5 MDa. One of 2 stacked pseudohexamers in the BMC. There are 20 BMC-T pseudohexamers per BMC, composed of mixed BMC-T1, BMC-T2 and BMC-T3. The shell facets are 20-30 Angstroms thick, with 1 of the stacked BMC-T trimers protruding to the exterior (PubMed:28642439, PubMed:30833088). The stacked trimers may serve as conduits to allow chemical flux across the protein shell, gated by Arg-70 which contacts Glu-69 in an adjacent subunit; they are flexible enough to play a role in accommodating variations in shell assembly (Probable).[1] [2] [3]
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
- ↑ 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