Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly.
Journal, issue, pages	Structure, Vol. 27, Issue 5, Page 749-763.e4, Year 2019
Publish date	May 7, 2019
Authors	Basil J Greber / Markus Sutter / Cheryl A Kerfeld /
PubMed Abstract	Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive ...Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive competitive advantages from their BMC-based catabolism, implicating BMCs as drug targets. BMC shells are of interest for bioengineering due to their diverse and selective permeability properties and because they self-assemble. A complete understanding of shell composition and organization is a prerequisite for biotechnological applications. Here, we report the cryoelectron microscopy structure of a BMC shell at 3.0-Å resolution, using an image-processing strategy that allowed us to determine the previously uncharacterized structural details of the interactions formed by the BMC-T and BMC-T shell subunits in the context of the assembled shell. We found unexpected structural plasticity among these interactions, resulting in distinct shell populations assembled from varying numbers of the BMC-T and BMC-T subunits. We discuss the implications of these findings on shell assembly and function.
External links	Structure / PubMed:30833088 / PubMed Central
Methods	EM (single particle)
Resolution	3.0 - 4.4 Å
Structure data	EMDB-9296: Cryo-EM structure of the HO BMC shell: Fully asymmetric reconstruction Method: EM (single particle) / Resolution: 4.4 Å 9307 6mzu EMDB-9307: Structure of the HO BMC shell: BMC-TD focused structure, closed state PDB-6mzu: Cryo-EM structure of the HO BMC shell: BMC-TD focused structure, closed state Method: EM (single particle) / Resolution: 3.4 Å 9308 6mzv EMDB-9308, PDB-6mzv: Cryo-EM structure of the HO BMC shell: BMC-TD focused structure, widened inner ring Method: EM (single particle) / Resolution: 3.4 Å 9309 6mzx EMDB-9309, PDB-6mzx: Cryo-EM structure of the HO BMC shell: Icosahedral reconstruction (main population) Method: EM (single particle) / Resolution: 3.0 Å 9310 6mzy EMDB-9310, PDB-6mzy: Cryo-EM structure of the HO BMC shell: Icosahedral reconstruction of the compacted subpopulation Method: EM (single particle) / Resolution: 3.3 Å 9311 6n06 EMDB-9311, PDB-6n06: Cryo-EM structure of the HO BMC shell: BMC-T1 in the assembled shell Method: EM (single particle) / Resolution: 3.4 Å 9312 6n07 EMDB-9312, PDB-6n07: Structure of the HO BMC shell: BMC-TD focused map, open inner pore, compacted shell Method: EM (single particle) / Resolution: 3.6 Å 9313 6n09 EMDB-9313, PDB-6n09: Cryo-EM structure of the HO BMC shell: subregion classified for BMC-T: TD-TDTDTD Method: EM (single particle) / Resolution: 3.5 Å 9314 6n0f EMDB-9314, PDB-6n0f: Cryo-EM structure of the HO BMC shell: subregion classified for BMC-T: TD-TSTSTS Method: EM (single particle) / Resolution: 3.9 Å 9315 6n0g EMDB-9315, PDB-6n0g: Cryo-EM structure of the HO BMC shell: subregion classified for BMC-T: TS-TDTDTD Method: EM (single particle) / Resolution: 3.6 Å
Source	haliangium ochraceum (bacteria) haliangium ochraceum (strain dsm 14365 / jcm 11303 / smp-2) (bacteria) haliangium ochraceum dsm 14365 (bacteria)
Keywords	STRUCTURAL PROTEIN / microcompartment / shell / compartmentalization / BMC fold / VIRUS LIKE PARTICLE