6xph | pdb_00006xph

CutR dimer with domain swap

spinqualitylabelsall models 6xph, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6xph is a 2 chain structure with sequence from Streptococcus intermedius atcc 27335. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, K, NA, SCN Related: 6xpi, 6xpj, 6xpk, 6xpl Gene: HMPREF1654_00416 (Streptococcus intermedius ATCC 27335) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Bacterial microcompartments are protein-based organelles that carry out specialized metabolic functions in diverse bacteria. Their outer shells are built from several thousand protein subunits. Some of the architectural principles of bacterial microcompartments have been articulated, with lateral packing of flat hexameric BMC proteins providing the basic foundation for assembly. Nonetheless, a complete understanding has been elusive, partly owing to polymorphic mechanisms of assembly exhibited by most microcompartment types. An earlier study of one homologous BMC shell protein subfamily, EutS/PduU, revealed a profoundly bent, rather than flat, hexameric structure. The possibility of a specialized architectural role was hypothesized, but artifactual effects of crystallization could not be ruled out. Here we report a series of crystal structures of an orthologous protein, CutR, from a glycyl-radical type choline-utilizing microcompartment from the bacterium Streptococcus intermedius. Depending on crystal form, expression construct, and minor mutations, a range of novel quaternary architectures was observed, including two spiral hexagonal assemblies. A new graphical approach helps illuminate the variations in BMC hexameric structure, with results substantiating the idea that the EutS/PduU/CutR subfamily of BMC proteins may endow microcompartment shells with flexible modes of assembly. Symmetry breaking and structural polymorphism in a bacterial microcompartment shell protein for choline utilization.,Ochoa JM, Nguyen VN, Nie M, Sawaya MR, Bobik TA, Yeates TO Protein Sci. 2020 Sep 4. doi: 10.1002/pro.3941. PMID:32885887 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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