6X6O
Crystal structure of T4 protein Spackle as determined by native SAD phasing
Summary for 6X6O
| Entry DOI | 10.2210/pdb6x6o/pdb |
| Descriptor | Protein spackle, CHLORIDE ION (3 entities in total) |
| Functional Keywords | apobec, deaminase, hydrolase, viral protein |
| Biological source | Escherichia virus T4 |
| Total number of polymer chains | 2 |
| Total formula weight | 24293.41 |
| Authors | Shi, K.,Kurniawan, F.,Banerjee, S.,Moeller, N.H.,Aihara, H. (deposition date: 2020-05-28, release date: 2020-09-16, Last modification date: 2024-10-09) |
| Primary citation | Shi, K.,Kurniawan, F.,Banerjee, S.,Moeller, N.H.,Aihara, H. Crystal structure of bacteriophage T4 Spackle as determined by native SAD phasing. Acta Crystallogr D Struct Biol, 76:899-904, 2020 Cited by PubMed 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. PubMed: 32876065DOI: 10.1107/S2059798320010979 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.52 Å) |
Structure validation
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