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1kpt

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(New page: 200px<br /><applet load="1kpt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kpt, resolution 1.75&Aring;" /> '''STRUCTURE AND FUNCTI...)
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[[Image:1kpt.jpg|left|200px]]<br /><applet load="1kpt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kpt, resolution 1.75&Aring;" />
 
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'''STRUCTURE AND FUNCTION OF A VIRALLY ENCODED FUNGAL TOXIN FROM USTILAGO MAYDIS: A FUNGAL AND MAMMALIAN CALCIUM CHANNEL INHIBITOR'''<br />
 
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==Overview==
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==STRUCTURE AND FUNCTION OF A VIRALLY ENCODED FUNGAL TOXIN FROM USTILAGO MAYDIS: A FUNGAL AND MAMMALIAN CALCIUM CHANNEL INHIBITOR==
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BACKGROUND: The P4 strain of the corn smut fungus, Ustilago maydis, secretes a fungal toxin, KP4, encoded by a fungal virus (UMV4) that, persistently infects its cells. UMV4, unlike most other (non-fungal), viruses, does not spread to uninfected cells by release into the, extracellular milieu during its normal life cycle and is thus dependent, upon host survival for replication. In symbiosis with the host fungus, UMV4 encodes KP4 to kill other competitive strains of U. maydis, thereby, promoting both host and virus survival. KP4 belongs to a family of fungal, toxins and determining its structure should lead to a better understanding, of the function and evolutionary origins of these toxins. Elucidation of, the mechanism of toxin action could lead to new anti-fungal agents against, human pathogens. RESULTS: We have determined the atomic structure of KP4, to 1.9 A resolution. KP4 belongs to the alpha/beta-sandwich family, and, has a unique topology comprising a five-stranded antiparallel beta-sheet, with two antiparallel alpha-helices lying at approximately 45 degrees to, these strands. The structure has two left-handed beta alpha beta, cross-overs and a basic protuberance extending from the beta-sheet. In, vivo experiments demonstrated abrogation of toxin killing by Ca2+ and, to, a lesser extent, Mg2+. These results led to experiments demonstrating that, the toxin specifically inhibits voltage-gated Ca2+ channels in mammalian, cells. CONCLUSIONS: Similarities, although somewhat limited, between KP4, and scorpion toxins led us to investigate the possibility that the toxic, effects of KP4 may be mediated by inhibition of cation channels. Our, results suggest that certain properties of fungal Ca2+ channels are, homologous to those in mammalian cells. KP4 may, therefore, be a new tool, for studying mammalian Ca2+ channels and current mammalian Ca2+ channel, inhibitors may be useful lead compounds for new anti-fungal agents.
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<StructureSection load='1kpt' size='340' side='right'caption='[[1kpt]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1kpt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ustilago_maydis Ustilago maydis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KPT FirstGlance]. <br>
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1KPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ustilago_maydis Ustilago maydis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KPT OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kpt OCA], [https://pdbe.org/1kpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kpt RCSB], [https://www.ebi.ac.uk/pdbsum/1kpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kpt ProSAT]</span></td></tr>
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==Reference==
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</table>
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Structure and function of a virally encoded fungal toxin from Ustilago maydis: a fungal and mammalian Ca2+ channel inhibitor., Gu F, Khimani A, Rane SG, Flurkey WH, Bozarth RF, Smith TJ, Structure. 1995 Aug 15;3(8):805-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7582897 7582897]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/KP4T_UMV4 KP4T_UMV4] This protein is lethal to sensitive cells of the same or related species. It specifically inhibits voltage-gated calcium channels. It inhibits cell growth and division by blocking calcium import.<ref>PMID:11532143</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kp/1kpt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kpt ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Ustilago maydis]]
[[Category: Ustilago maydis]]
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[[Category: Gu, F.]]
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[[Category: Gu F]]
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[[Category: Smith, T.]]
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[[Category: Smith T]]
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[[Category: alpha/beta family]]
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[[Category: fungal toxin]]
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[[Category: killer toxin]]
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[[Category: left-handed crossover]]
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[[Category: single subunit]]
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[[Category: ustilago maydis]]
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[[Category: virally encoded]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:36:07 2007''
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Current revision

STRUCTURE AND FUNCTION OF A VIRALLY ENCODED FUNGAL TOXIN FROM USTILAGO MAYDIS: A FUNGAL AND MAMMALIAN CALCIUM CHANNEL INHIBITOR

PDB ID 1kpt

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