6X6O

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

6X6O の概要

• エントリーDOI: 10.2210/pdb6x6o/pdb
• 分子名称: Protein spackle, CHLORIDE ION (3 entities in total)
• 機能のキーワード: apobec, deaminase, hydrolase, viral protein
• 由来する生物種: Escherichia virus T4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24293.41

構造登録者

Shi, K.,Kurniawan, F.,Banerjee, S.,Moeller, N.H.,Aihara, H. (登録日: 2020-05-28, 公開日: 2020-09-16, 最終更新日: 2024-10-09)

主引用文献

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

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: 32876065
DOI: 10.1107/S2059798320010979

実験手法

X-RAY DIFFRACTION (1.52 Å)