6x6o

Crystal structure of T4 protein Spackle as determined by native SAD phasing

spinqualitylabelsall models 6x6o, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.52Å Ligands: CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The crystal structure of a bacteriophage T4 early gene product, Spackle, was determined by native sulfur single-wavelength anomalous diffraction (SAD) phasing using synchrotron radiation and was refined to 1.52 A resolution. The structure shows that Spackle consists of a bundle of five alpha-helices, forming a relatively flat disc-like overall shape. Although Spackle forms a dimer in the crystal, size-exclusion chromatography with multi-angle light scattering shows that it is monomeric in solution. Mass spectrometry confirms that purified mature Spackle lacks the amino-terminal signal peptide and contains an intramolecular disulfide bond, consistent with its proposed role in the periplasm of T4 phage-infected Escherichia coli cells. The surface electrostatic potential of Spackle shows a strikingly bipolar charge distribution, suggesting a possible mode of membrane association and inhibition of the tail lysozyme activity in T4 bacteriophage superinfection exclusion. Crystal structure of bacteriophage T4 Spackle as determined by native SAD phasing.,Shi K, Kurniawan F, Banerjee S, Moeller NH, Aihara H Acta Crystallogr D Struct Biol. 2020 Sep 1;76(Pt 9):899-904. doi:, 10.1107/S2059798320010979. Epub 2020 Aug 25. PMID:32876065 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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