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Crystal structure of bacteriophage T4 Spackle as determined by native SAD phasing.


ABSTRACT: 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 Å resolution. The structure shows that Spackle consists of a bundle of five α-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.

SUBMITTER: Shi K 

PROVIDER: S-EPMC7466748 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

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Crystal structure of bacteriophage T4 Spackle as determined by native SAD phasing.

Shi Ke K   Kurniawan Fredy F   Banerjee Surajit S   Moeller Nicholas H NH   Aihara Hideki H  

Acta crystallographica. Section D, Structural biology 20200825 Pt 9


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 Å resolution. The structure shows that Spackle consists of a bundle of five α-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.  ...[more]

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