Structural highlights
Function
[THN3_VISAL] Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of viscotoxin A3 (VT A3) extracted from European mistletoe (Viscum album L.) has been solved using the anomalous diffraction of the native S atoms measured in-house with Cu Kalpha radiation to a resolution of 2.2 A and truncated to 2.5 A. A 1.75 A resolution synchrotron data set was used for phase expansion and refinement. An innovation in the dual-space substructure-solution program SHELXD enabled the individual S atoms of the disulfide bonds to be located using the Cu Kalpha data; this resulted in a marked improvement in the phasing compared with the use of super-S atoms. The VT A3 monomer consists of 46 amino acids with three disulfide bridges and has an overall fold resembling the canonical architecture of the alpha- and beta-thionins, a capital letter L. The asymmetric unit consists of two monomers related by a local twofold axis and held together by hydrophobic interactions between the monomer units. One phosphate anion (confirmed by 31P-NMR and MS) is associated with each monomer.
Structure of viscotoxin A3: disulfide location from weak SAD data.,Debreczeni JE, Girmann B, Zeeck A, Kratzner R, Sheldrick GM Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2125-32. Epub 2003, Nov 27. PMID:14646070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Debreczeni JE, Girmann B, Zeeck A, Kratzner R, Sheldrick GM. Structure of viscotoxin A3: disulfide location from weak SAD data. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2125-32. Epub 2003, Nov 27. PMID:14646070
