4N3E
Crystal structure of Hyp-1, a St John's wort PR-10 protein, in complex with 8-anilino-1-naphthalene sulfonate (ANS)
Summary for 4N3E
| Entry DOI | 10.2210/pdb4n3e/pdb |
| Related | 1BV1 1FM4 1ICX 1IFV 1XDF 2FLH 2QIM 3E85 3IE5 3US7 4A80 4A81 4A83 4A85 4A86 4A87 4A8U 4A8V 4GY9 4JHG |
| Descriptor | Phenolic oxidative coupling protein, 8-ANILINO-1-NAPHTHALENE SULFONATE, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (5 entities in total) |
| Functional Keywords | plant hormone binding, phytohormone binding, cytokinin, plant defense, pathogenesis-related protein, pr-10 protein, hypericin, depression, pr-10 fold, hydrophobic cavity, glycine-rich loop, ans displacement assay (ada), commensurately modulated superstructure, tetartohedral twinning, plant protein |
| Biological source | Hypericum perforatum (St. John's wort) |
| Total number of polymer chains | 28 |
| Total formula weight | 545269.47 |
| Authors | Sliwiak, J.,Dauter, Z.,Mccoy, A.J.,Read, R.J.,Jaskolski, M. (deposition date: 2013-10-07, release date: 2014-02-26, Last modification date: 2023-09-20) |
| Primary citation | Sliwiak, J.,Jaskolski, M.,Dauter, Z.,McCoy, A.J.,Read, R.J. Likelihood-based molecular-replacement solution for a highly pathological crystal with tetartohedral twinning and sevenfold translational noncrystallographic symmetry. Acta Crystallogr.,Sect.D, 70:471-480, 2014 Cited by PubMed Abstract: Translational noncrystallographic symmetry (tNCS) is a pathology of protein crystals in which multiple copies of a molecule or assembly are found in similar orientations. Structure solution is problematic because this breaks the assumptions used in current likelihood-based methods. To cope with such cases, new likelihood approaches have been developed and implemented in Phaser to account for the statistical effects of tNCS in molecular replacement. Using these new approaches, it was possible to solve the crystal structure of a protein exhibiting an extreme form of this pathology with seven tetrameric assemblies arrayed along the c axis. To resolve space-group ambiguities caused by tetartohedral twinning, the structure was initially solved by placing 56 copies of the monomer in space group P1 and using the symmetry of the solution to define the true space group, C2. The resulting structure of Hyp-1, a pathogenesis-related class 10 (PR-10) protein from the medicinal herb St John's wort, reveals the binding modes of the fluorescent probe 8-anilino-1-naphthalene sulfonate (ANS), providing insight into the function of the protein in binding or storing hydrophobic ligands. PubMed: 24531481DOI: 10.1107/S1399004713030319 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.43 Å) |
Structure validation
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