1kp6

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Revision as of 20:26, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1kp6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kp6, resolution 1.80Å" /> '''USTILAGO MAYDIS KILL...)
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1kp6, resolution 1.80Å

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USTILAGO MAYDIS KILLER TOXIN KP6 ALPHA-SUBUNIT

OverviewOverview

Ustilago maydis is a fungal pathogen of maize, some strains of which, secrete killer toxins. The toxins are encoded by double-stranded RNA, viruses in the cell cytoplasm. The U. maydis killer toxin KP6 contains two, polypeptide chains, alpha and beta, having 79 and 81 amino acids, respectively, both of which are necessary for its killer activity. The, crystal structure of the alpha-subunit of KP6 (KP6alpha) has been, determined at 1.80-A resolution. KP6alpha forms a single domain structure, that has an overall shape of an ellipsoid with dimensions 40 A x 26 A x 21, A and belongs to the alpha/beta-sandwich family. The tertiary structure, consists of a four-stranded antiparallel beta-sheet, a pair of, antiparallel alpha-helices, a short strand along one edge of the sheet, and a short N-terminal helix. Although the fold is reminiscent of toxins, of similar size, the topology of KP6alpha is distinctly different in that, the alpha/beta-sandwich motif has two right-handed betaalphabeta split, crossovers. Monomers of KP6alpha assemble through crystallographic, symmetries, forming a hexamer with a central pore lined by hydrophobic, N-terminal helices. The central pore could play an important role in the, mechanism of the killing action of the toxin.

About this StructureAbout this Structure

1KP6 is a Single protein structure of sequence from Ustilago maydis with SO4 as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of Ustilago maydis killer toxin KP6 alpha-subunit. A multimeric assembly with a central pore., Li N, Erman M, Pangborn W, Duax WL, Park CM, Bruenn J, Ghosh D, J Biol Chem. 1999 Jul 16;274(29):20425-31. PMID:10400668

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