1okh
From Proteopedia
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VISCOTOXIN A3 FROM VISCUM ALBUM L.
Overview
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.
About this Structure
1OKH is a Single protein structure of sequence from Viscum album with PO4 and SO4 as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 5 16:57:38 2007
Categories: Single protein | Viscum album | Debreczeni, J.E. | Girmann, B. | Sheldrick, G.M. | Zeeck, A. | PO4 | SO4 | Plant defense | Thionin | Toxin
