6ner

Synthetic Haliangium ochraceum BMC shell

spinqualitylabelsall models 6ner, resolution 3.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ner is a 30 chain structure with sequence from Haliangium ochraceum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.59Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. Publication Abstract from PubMed Bacterial microcompartments are subcellular compartments found in many prokaryotes; they consist of a protein shell that encapsulates enzymes that perform a variety of functions. The shell protects the cell from potentially toxic intermediates and colocalizes enzymes for higher efficiency. Accordingly, it is of considerable interest for biotechnological applications. We have previously structurally characterized an intact 40 nm shell comprising three different types of proteins. One of those proteins, BMC-H, forms a cyclic hexamer; here we have engineered a synthetic protein that consists of a tandem duplication of BMC-H connected by a short linker. The synthetic protein forms cyclic trimers that self-assemble to form a smaller (25 nm) icosahedral shell with gaps at the pentamer positions. When coexpressed in vivo with the pentamer fused to an affinity tag we can purify complete icosahedral shells. This engineered shell protein constitutes a minimal shell system to study permeability; reducing symmetry from 6- to 3-fold will allow for finer control of the pore environment. We have determined a crystal structure of this shell to guide rational engineering of this microcompartment shell for biotechnological applications. Structural Characterization of a Synthetic Tandem-Domain Bacterial Microcompartment Shell Protein Capable of Forming Icosahedral Shell Assemblies.,Sutter M, McGuire S, Ferlez B, Kerfeld CA ACS Synth Biol. 2019 Mar 27. doi: 10.1021/acssynbio.9b00011. PMID:30901520 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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