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| | ==SOLUTION STRUCTURE OF NEUROTOXIN I FROM THE SEA ANEMONE STICHODACTYLA HELIANTHUS. A NUCLEAR MAGNETIC RESONANCE, DISTANCE GEOMETRY AND RESTRAINED MOLECULAR DYNAMICS STUDY== | | ==SOLUTION STRUCTURE OF NEUROTOXIN I FROM THE SEA ANEMONE STICHODACTYLA HELIANTHUS. A NUCLEAR MAGNETIC RESONANCE, DISTANCE GEOMETRY AND RESTRAINED MOLECULAR DYNAMICS STUDY== |
| - | <StructureSection load='1sh1' size='340' side='right'caption='[[1sh1]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1sh1' size='340' side='right'caption='[[1sh1]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sh1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinia_helianthus Actinia helianthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SH1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SH1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Stichodactyla_helianthus Stichodactyla helianthus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SH1 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2sh1|2sh1]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sh1 OCA], [http://pdbe.org/1sh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sh1 RCSB], [http://www.ebi.ac.uk/pdbsum/1sh1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sh1 ProSAT]</span></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=1sh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sh1 OCA], [https://pdbe.org/1sh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sh1 RCSB], [https://www.ebi.ac.uk/pdbsum/1sh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sh1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TXA1_STOHE TXA1_STOHE]] Binds specifically to the sodium channel (Nav), thereby delaying its inactivation during signal transduction. Selectively toxic to crustaceans.<ref>PMID:7913833</ref> | + | [https://www.uniprot.org/uniprot/NA21_STIHL NA21_STIHL] Binds specifically to voltage-gated sodium channels (Nav), thereby delaying their inactivation during signal transduction (By similarity). Is highly toxic to crabs (by intrahemocoelic injection) (PubMed:2568126, PubMed:22015268), but without effect upon mice (by intraperitoneal injection) (PubMed:2568126).<ref>PMID:22015268</ref> <ref>PMID:2568126</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sh/1sh1_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sh/1sh1_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinia helianthus]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fogh, R H]] | + | [[Category: Stichodactyla helianthus]] |
| - | [[Category: Norton, R S]] | + | [[Category: Fogh RH]] |
| - | [[Category: Neurotoxin]] | + | [[Category: Norton RS]] |
| Structural highlights
Function
NA21_STIHL Binds specifically to voltage-gated sodium channels (Nav), thereby delaying their inactivation during signal transduction (By similarity). Is highly toxic to crabs (by intrahemocoelic injection) (PubMed:2568126, PubMed:22015268), but without effect upon mice (by intraperitoneal injection) (PubMed:2568126).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of the sea anemone polypeptide Stichodactyla helianthus neurotoxin I in aqueous solution has been determined using distance geometry and restrained molecular dynamics simulations based on NMR data acquired at 500 MHz. A set of 470 nuclear Overhauser enhancement values was measured, of which 216 were used as distance restraints in the structure determination along with 15 dihedral angles derived from coupling constants. After restrained molecular dynamics refinement, the eight structures that best fit the input data form a closely related family. They describe a structure that consists of a core of twisted, four-stranded, antiparallel beta-sheet encompassing residues 1-3, 19-24, 29-34, and 40-47, joined by three loops, two of which are well defined by the NMR data. The third loop, encompassing residues 7-16, is poorly defined by the data and is assumed to undergo conformational averaging in solution. Pairwise root mean square displacement values for the backbone heavy atoms of the eight best structures are 1.3 +/- 0.2A when the poorly defined loop is excluded and 3.6 +/- 1.0A for all backbone atoms. Refinement using restrained molecular dynamics improved the quality of the structures generated by distance geometry calculations with respect to the number of nuclear Overhauser enhancements violated, the size of the total distance violations and the total potential energies of the structures. The family of structures for S. heliathus neurotoxin I is compared with structures of related sea anemone proteins that also bind to the voltage-gated sodium channel.
Solution structure of neurotoxin I from the sea anemone Stichodactyla helianthus. A nuclear magnetic resonance, distance geometry, and restrained molecular dynamics study.,Fogh RH, Kem WR, Norton RS J Biol Chem. 1990 Aug 5;265(22):13016-28. PMID:1973932[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rodríguez AA, Cassoli JS, Sa F, Dong ZQ, de Freitas JC, Pimenta AM, de Lima ME, Konno K, Lee SM, Garateix A, Zaharenko AJ. Peptide fingerprinting of the neurotoxic fractions isolated from the secretions of sea anemones Stichodactyla helianthus and Bunodosoma granulifera. New members of the APETx-like family identified by a 454 pyrosequencing approach. Peptides. 2012 Mar;34(1):26-38. PMID:22015268 doi:10.1016/j.peptides.2011.10.011
- ↑ Kem WR, Parten B, Pennington MW, Price DA, Dunn BM. Isolation, characterization, and amino acid sequence of a polypeptide neurotoxin occurring in the sea anemone Stichodactyla helianthus. Biochemistry. 1989 Apr 18;28(8):3483-9. PMID:2568126 doi:10.1021/bi00434a050
- ↑ Fogh RH, Kem WR, Norton RS. Solution structure of neurotoxin I from the sea anemone Stichodactyla helianthus. A nuclear magnetic resonance, distance geometry, and restrained molecular dynamics study. J Biol Chem. 1990 Aug 5;265(22):13016-28. PMID:1973932
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