1kp6: Difference between revisions
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[[ | ==USTILAGO MAYDIS KILLER TOXIN KP6 ALPHA-SUBUNIT== | ||
<StructureSection load='1kp6' size='340' side='right' caption='[[1kp6]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1kp6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ustilago_maydis Ustilago maydis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KP6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KP6 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kp6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kp6 RCSB], [http://www.ebi.ac.uk/pdbsum/1kp6 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:10400668</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Ustilago maydis]] | [[Category: Ustilago maydis]] | ||
[[Category: Bruenn, J.]] | [[Category: Bruenn, J.]] | ||
Revision as of 20:36, 28 September 2014
USTILAGO MAYDIS KILLER TOXIN KP6 ALPHA-SUBUNITUSTILAGO MAYDIS KILLER TOXIN KP6 ALPHA-SUBUNIT
Structural highlights
Publication Abstract from PubMedUstilago 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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