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ANS complex of St John’s wort PR-10 protein with 28 copies in the asymmetric unit: a fiendish combination of pseudosymmetry with tetartohedral twinning

Journal Article · · Acta Crystallographica. Section D: Biological Crystallography
 [1];  [2];  [3]; ;  [4];  [1]
  1. Polish Academy of Sciences, Poznan (Poland)
  2. National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439 (United States)
  3. Poznan University of Medical Sciences, Poznan (Poland)
  4. University of Cambridge, Cambridge CB2 0XY (United Kingdom)

Hyp-1, a pathogenesis-related class 10 (PR-10) protein from H. perforatum, was crystallized in complex with the fluorescent probe 8-anilino-1-naphthalene sulfonate (ANS). The asymmetric unit of the tetartohedrally twinned crystal contains 28 copies of the protein arranged in columns with noncrystallographic sevenfold translational symmetry and with additional pseudotetragonal rotational NCS. Hyp-1, a pathogenesis-related class 10 (PR-10) protein from St John’s wort (Hypericum perforatum), was crystallized in complex with the fluorescent probe 8-anilino-1-naphthalene sulfonate (ANS). The highly pseudosymmetric crystal has 28 unique protein molecules arranged in columns with sevenfold translational noncrystallographic symmetry (tNCS) along c and modulated X-ray diffraction with intensity crests at l = 7n and l = 7n ± 3. The translational NCS is combined with pseudotetragonal rotational NCS. The crystal was a perfect tetartohedral twin, although detection of twinning was severely hindered by the pseudosymmetry. The structure determined at 2.4 Å resolution reveals that the Hyp-1 molecules (packed as β-sheet dimers) have three novel ligand-binding sites (two internal and one in a surface pocket), which was confirmed by solution studies. In addition to 60 Hyp-1-docked ligands, there are 29 interstitial ANS molecules distributed in a pattern that violates the arrangement of the protein molecules and is likely to be the generator of the structural modulation. In particular, whenever the stacked Hyp-1 molecules are found closer together there is an ANS molecule bridging them.

OSTI ID:
22347699
Journal Information:
Acta Crystallographica. Section D: Biological Crystallography, Journal Name: Acta Crystallographica. Section D: Biological Crystallography Journal Issue: Pt 4 Vol. 71; ISSN ABCRE6; ISSN 0907-4449
Country of Publication:
Denmark
Language:
English

Cited By (2)

Characterizing pathological imperfections in macromolecular crystals: lattice disorders and modulations journal December 2019
Supercell refinement: a cautionary tale journal August 2019

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