4JP7
High resolution structure of a papaya barwin-like protein (crystal form 2)
Summary for 4JP7
| Entry DOI | 10.2210/pdb4jp7/pdb |
| Related | 4JP6 |
| Descriptor | papaya barwin-like protein, GLYCEROL (3 entities in total) |
| Functional Keywords | pathogenesis-related protein of family 4, barwin family, double-psi beta barrel, unknown function |
| Biological source | Carica papaya |
| Total number of polymer chains | 2 |
| Total formula weight | 27422.56 |
| Authors | Wohlkonig, A.,Wintjens, R. (deposition date: 2013-03-19, release date: 2013-10-02, Last modification date: 2024-10-16) |
| Primary citation | Huet, J.,Teinkela Mbosso, E.J.,Soror, S.,Meyer, F.,Looze, Y.,Wintjens, R.,Wohlkonig, A. High-resolution structure of a papaya plant-defence barwin-like protein solved by in-house sulfur-SAD phasing. Acta Crystallogr.,Sect.D, 69:2017-2026, 2013 Cited by PubMed Abstract: The first crystal structure of a barwin-like protein, named carwin, has been determined at high resolution by single-wavelength anomalous diffraction (SAD) phasing using the six intrinsic S atoms present in the protein. The barwin-like protein was purified from Carica papaya latex and crystallized in the orthorhombic space group P212121. Using in-house Cu Kα X-ray radiation, 16 cumulative diffraction data sets were acquired to increase the signal-to-noise level and thereby the anomalous scattering signal. A sequence-database search on the papaya genome identified two carwin isoforms of 122 residues in length, both containing six S atoms that yield an estimated Bijvoet ratio of 0.93% at 1.54 Å wavelength. A systematic analysis of data quality and redundancy was performed to assess the capacity to locate the S atoms and to phase the data. It was observed that the crystal decay was low during data collection and that successful S-SAD phasing could be obtained with a relatively low data multiplicity of about 7. Using a synchrotron source, high-resolution data (1 Å) were collected from two different crystal forms of the papaya latex carwin. The refined structures showed a central β-barrel of six strands surrounded by several α-helices and loops. The β-barrel of carwin appears to be a common structural module that is shared within several other unrelated proteins. Finally, the possible biological function of the protein is discussed. PubMed: 24100320DOI: 10.1107/S0907444913018015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.05 Å) |
Structure validation
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