1okh | pdb_00001okh
VISCOTOXIN A3 FROM VISCUM ALBUM L.
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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. Known structural/functional 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 Sun Feb 3 09:59:16 2008
