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1sn4

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(New page: 200px<br /><applet load="1sn4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sn4, resolution 1.3&Aring;" /> '''STRUCTURE OF SCORPION...)
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[[Image:1sn4.jpg|left|200px]]<br /><applet load="1sn4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sn4, resolution 1.3&Aring;" />
 
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'''STRUCTURE OF SCORPION NEUROTOXIN BMK M4'''<br />
 
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==Overview==
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==STRUCTURE OF SCORPION NEUROTOXIN BMK M4==
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The crystal structures of two group III alpha-like toxins from the, scorpion Buthus martensii Karsch, BmK M1 and BmK M4, were determined at, 1.7 A and 1.3 A resolution and refined to R factors of 0.169 and 0.166, respectively. The first high-resolution structures of the alpha-like, scorpion toxin show some striking features compared with structures of the, "classical" alpha-toxin. Firstly, a non-proline cis peptide bond between, residues 9 and 10 unusually occurs in the five-member reverse turn 8-12., Secondly, the cis peptide 9-10 mediates the spatial relationship between, the turn 8-12 and the C-terminal stretch 58-64 through a pair of, main-chain hydrogen bonds between residues 10 and 64 to form a unique, tertiary arrangement which features the special orientation of the, terminal residues 62-64. Finally, in consequence of the peculiar, orientation of the C-terminal residues, the functional groups of Arg58, which are crucial for the toxin-receptor interaction, are exposed and, accessible in BmK M1 and M4 rather than buried as in the classical, alpha-toxins. Sequence alignment and characteristics analysis suggested, that the above structural features observed in BmK M1 and M4 occur in all, group III alpha-like toxins. Recently, some group III alpha-like toxins, were demonstrated to occupy a receptor site different from the classical, alpha-toxin. Therefore, the distinct structural features of BmK M1 and M4, presented here may provide the structural basis for the newly recognized, toxin-receptor binding site selectivity. Besides, the non-proline cis, peptide bonds found in these two structures play a role in the formation, of the structural characteristics and in keeping accurate positions of the, functionally crucial residues. This manifested a way to achieve high, levels of molecular specificity and atomic precision through the strained, backbone geometry.
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<StructureSection load='1sn4' size='340' side='right'caption='[[1sn4]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1sn4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SN4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SN4 FirstGlance]. <br>
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1SN4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SN4 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]] 1.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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==Reference==
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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=1sn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sn4 OCA], [https://pdbe.org/1sn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sn4 RCSB], [https://www.ebi.ac.uk/pdbsum/1sn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sn4 ProSAT]</span></td></tr>
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Crystal structures of two alpha-like scorpion toxins: non-proline cis peptide bonds and implications for new binding site selectivity on the sodium channel., He XL, Li HM, Zeng ZH, Liu XQ, Wang M, Wang DC, J Mol Biol. 1999 Sep 10;292(1):125-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10493862 10493862]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SCX4_MESMA SCX4_MESMA] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active against mammals.
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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/sn/1sn4_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=1sn4 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mesobuthus martensii]]
[[Category: Mesobuthus martensii]]
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[[Category: Single protein]]
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[[Category: He XL]]
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[[Category: He, X.L.]]
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[[Category: Li HM]]
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[[Category: Li, H.M.]]
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[[Category: Liu XQ]]
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[[Category: Liu, X.Q.]]
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[[Category: Wang DC]]
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[[Category: Wang, D.C.]]
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[[Category: Zeng ZH]]
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[[Category: Zeng, Z.H.]]
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[[Category: ACT]]
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[[Category: neurotoxin]]
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[[Category: scorpion]]
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[[Category: sodium channel inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:30:21 2007''
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Current revision

STRUCTURE OF SCORPION NEUROTOXIN BMK M4

PDB ID 1sn4

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