1b3c
From Proteopedia
(Difference between revisions)
| (15 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1b3c.gif|left|200px]]<br /><applet load="1b3c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1b3c" /> | ||
| - | '''SOLUTION STRUCTURE OF A BETA-NEUROTOXIN FROM THE NEW WORLD SCORPION CENTRUROIDES SCULPTURATUS EWING'''<br /> | ||
| - | == | + | ==SOLUTION STRUCTURE OF A BETA-NEUROTOXIN FROM THE NEW WORLD SCORPION CENTRUROIDES SCULPTURATUS EWING== |
| + | <StructureSection load='1b3c' size='340' side='right'caption='[[1b3c]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1b3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Centruroides_sculpturatus Centruroides sculpturatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B3C FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 40 models</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b3c OCA], [https://pdbe.org/1b3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b3c RCSB], [https://www.ebi.ac.uk/pdbsum/1b3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b3c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SCXI_CENSC SCXI_CENSC] Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. Affects channels from chicken and frog. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/1b3c_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1b3c ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
We report the detailed solution structure of the 7.2 kDa protein CsE-I, a beta-neurotoxin from the New World scorpion Centruroides sculpturatus Ewing. This toxin binds to sodium channels, but unlike the alpha-neurotoxins, shifts the voltage of activation toward more negative potentials causing the membrane to fire spontaneously. Sequence-specific proton NMR assignments were made using 600 MHz 2D-NMR data. Distance geometry and dynamical simulated annealing refinements were performed using experimental distance and torsion angle constraints from NOESY and pH-COSY data. A family of 40 structures without constraint violations was generated, and an energy-minimized average structure was computed. The backbone conformation of the CsE-I toxin shows similar secondary structural features as the prototypical alpha-neurotoxin, CsE-v3, and is characterized by a short 2(1/2)-turn alpha-helix and a 3-strand antiparallel beta-sheet, both held together by disulfide bridges. The RMSD for the backbone atoms between CsE-I and CsE-v3 is 1.48 A. Despite this similarity in the overall backbone folding, the these two proteins show some important differences in the primary structure (sequence) and electrostatic potential surfaces. Our studies provide a basis for unravelling the role of these differences in relation to the known differences in the receptor sites on the voltage sensitive sodium channel for the alpha- and beta-neurotoxins. | We report the detailed solution structure of the 7.2 kDa protein CsE-I, a beta-neurotoxin from the New World scorpion Centruroides sculpturatus Ewing. This toxin binds to sodium channels, but unlike the alpha-neurotoxins, shifts the voltage of activation toward more negative potentials causing the membrane to fire spontaneously. Sequence-specific proton NMR assignments were made using 600 MHz 2D-NMR data. Distance geometry and dynamical simulated annealing refinements were performed using experimental distance and torsion angle constraints from NOESY and pH-COSY data. A family of 40 structures without constraint violations was generated, and an energy-minimized average structure was computed. The backbone conformation of the CsE-I toxin shows similar secondary structural features as the prototypical alpha-neurotoxin, CsE-v3, and is characterized by a short 2(1/2)-turn alpha-helix and a 3-strand antiparallel beta-sheet, both held together by disulfide bridges. The RMSD for the backbone atoms between CsE-I and CsE-v3 is 1.48 A. Despite this similarity in the overall backbone folding, the these two proteins show some important differences in the primary structure (sequence) and electrostatic potential surfaces. Our studies provide a basis for unravelling the role of these differences in relation to the known differences in the receptor sites on the voltage sensitive sodium channel for the alpha- and beta-neurotoxins. | ||
| - | + | Solution structure of a beta-neurotoxin from the New World scorpion Centruroides sculpturatus Ewing.,Jablonsky MJ, Jackson PL, Trent JO, Watt DD, Krishna NR Biochem Biophys Res Commun. 1999 Jan 19;254(2):406-12. PMID:9918851<ref>PMID:9918851</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1b3c" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Centruroides sculpturatus]] | [[Category: Centruroides sculpturatus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Jablonsky | + | [[Category: Jablonsky MJ]] |
| - | [[Category: Jackson | + | [[Category: Jackson PL]] |
| - | [[Category: Krishna | + | [[Category: Krishna NR]] |
| - | [[Category: Trent | + | [[Category: Trent JO]] |
| - | [[Category: Watt | + | [[Category: Watt DD]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
SOLUTION STRUCTURE OF A BETA-NEUROTOXIN FROM THE NEW WORLD SCORPION CENTRUROIDES SCULPTURATUS EWING
| |||||||||||
