1wt8: Difference between revisions

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New page: left|200px<br /><applet load="1wt8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wt8" /> '''Solution Structure of BmP08 from the Venom o...
 
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[[Image:1wt8.gif|left|200px]]<br /><applet load="1wt8" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution Structure of BmP08 from the Venom of Scorpion Buthus martensii Karsch, 20 structures'''<br />


==Overview==
==Solution Structure of BmP08 from the Venom of Scorpion Buthus martensii Karsch, 20 structures==
A novel short-chain scorpion toxin BmP08 was purified from the venom of, the Chinese scorpion Buthus martensi Karsch by a combination of, gel-filtration, ion exchange, and reversed-phase chromatography. The, primary sequence of BmP08 was determined using the tandem MS/MS technique, and Edman degradation, as well as results of NMR sequential assignments., It is composed of 31 amino acid residues including six cysteine residues, and shares less than 25% sequence identity with the known alpha-KTx, toxins. BmP08 shows no inhibitory activity on all tested voltage-dependent, and Ca(2+)-activated potassium channels. The 3D-structure of BmP08 has, been determined by 2D-NMR spectroscopy and molecular modeling techniques., This toxin adopts a common alpha/beta-motif, but shows a distinctive local, conformation and features a 3(10)-helix and a shorter beta-sheet. The, unique structure is closely related to the distinct primary sequence of, the toxin, especially to the novel arrangement of S-S linkages in the, molecule, in which two disulfide bridges (C(i)-C(j) and C(i+3)-C(j+3)), link covalently the 3(10)-helix with one strand of the beta-sheet, structure. The electrostatic potential surface analysis of the toxin, reveals salt bridges and hydrogen bonds between the basic residues and, negatively charged residues nearby in BmP08, which may be unfavorable for, its binding with the known voltage-dependent and Ca(2+)-activated, potassium channels. Thus, finding the target for this toxin should be an, interesting task in the future.
<StructureSection load='1wt8' size='340' side='right'caption='[[1wt8]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wt8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WT8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=1wt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wt8 OCA], [https://pdbe.org/1wt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wt8 RCSB], [https://www.ebi.ac.uk/pdbsum/1wt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wt8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SCKI_MESMA SCKI_MESMA] Does not show any effect on Na(+), Ca(2+) currents, nor on voltage-gated and calcium-activated potassium channels.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A novel short-chain scorpion toxin BmP08 was purified from the venom of the Chinese scorpion Buthus martensi Karsch by a combination of gel-filtration, ion exchange, and reversed-phase chromatography. The primary sequence of BmP08 was determined using the tandem MS/MS technique and Edman degradation, as well as results of NMR sequential assignments. It is composed of 31 amino acid residues including six cysteine residues and shares less than 25% sequence identity with the known alpha-KTx toxins. BmP08 shows no inhibitory activity on all tested voltage-dependent and Ca(2+)-activated potassium channels. The 3D-structure of BmP08 has been determined by 2D-NMR spectroscopy and molecular modeling techniques. This toxin adopts a common alpha/beta-motif, but shows a distinctive local conformation and features a 3(10)-helix and a shorter beta-sheet. The unique structure is closely related to the distinct primary sequence of the toxin, especially to the novel arrangement of S-S linkages in the molecule, in which two disulfide bridges (C(i)-C(j) and C(i+3)-C(j+3)) link covalently the 3(10)-helix with one strand of the beta-sheet structure. The electrostatic potential surface analysis of the toxin reveals salt bridges and hydrogen bonds between the basic residues and negatively charged residues nearby in BmP08, which may be unfavorable for its binding with the known voltage-dependent and Ca(2+)-activated potassium channels. Thus, finding the target for this toxin should be an interesting task in the future.


==About this Structure==
Solution structure of BmP08, a novel short-chain scorpion toxin from Buthus martensi Karsch.,Chen X, Li Y, Tong X, Zhang N, Wu G, Zhang Q, Wu H Biochem Biophys Res Commun. 2005 May 20;330(4):1116-26. PMID:15823559<ref>PMID:15823559</ref>
1WT8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WT8 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of BmP08, a novel short-chain scorpion toxin from Buthus martensi Karsch., Chen X, Li Y, Tong X, Zhang N, Wu G, Zhang Q, Wu H, Biochem Biophys Res Commun. 2005 May 20;330(4):1116-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15823559 15823559]
</div>
<div class="pdbe-citations 1wt8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mesobuthus martensii]]
[[Category: Mesobuthus martensii]]
[[Category: Single protein]]
[[Category: Chen X]]
[[Category: Chen, X.]]
[[Category: Li Y]]
[[Category: Li, Y.]]
[[Category: Tong X]]
[[Category: Tong, X.]]
[[Category: Wu G]]
[[Category: Wu, G.]]
[[Category: Wu H]]
[[Category: Wu, H.]]
[[Category: Zhang N]]
[[Category: Zhang, N.]]
[[Category: alpha/beta scaffold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:39:28 2007''

Latest revision as of 10:42, 23 October 2024

Solution Structure of BmP08 from the Venom of Scorpion Buthus martensii Karsch, 20 structuresSolution Structure of BmP08 from the Venom of Scorpion Buthus martensii Karsch, 20 structures

Structural highlights

1wt8 is a 1 chain structure with sequence from Mesobuthus martensii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCKI_MESMA Does not show any effect on Na(+), Ca(2+) currents, nor on voltage-gated and calcium-activated potassium channels.

Publication Abstract from PubMed

A novel short-chain scorpion toxin BmP08 was purified from the venom of the Chinese scorpion Buthus martensi Karsch by a combination of gel-filtration, ion exchange, and reversed-phase chromatography. The primary sequence of BmP08 was determined using the tandem MS/MS technique and Edman degradation, as well as results of NMR sequential assignments. It is composed of 31 amino acid residues including six cysteine residues and shares less than 25% sequence identity with the known alpha-KTx toxins. BmP08 shows no inhibitory activity on all tested voltage-dependent and Ca(2+)-activated potassium channels. The 3D-structure of BmP08 has been determined by 2D-NMR spectroscopy and molecular modeling techniques. This toxin adopts a common alpha/beta-motif, but shows a distinctive local conformation and features a 3(10)-helix and a shorter beta-sheet. The unique structure is closely related to the distinct primary sequence of the toxin, especially to the novel arrangement of S-S linkages in the molecule, in which two disulfide bridges (C(i)-C(j) and C(i+3)-C(j+3)) link covalently the 3(10)-helix with one strand of the beta-sheet structure. The electrostatic potential surface analysis of the toxin reveals salt bridges and hydrogen bonds between the basic residues and negatively charged residues nearby in BmP08, which may be unfavorable for its binding with the known voltage-dependent and Ca(2+)-activated potassium channels. Thus, finding the target for this toxin should be an interesting task in the future.

Solution structure of BmP08, a novel short-chain scorpion toxin from Buthus martensi Karsch.,Chen X, Li Y, Tong X, Zhang N, Wu G, Zhang Q, Wu H Biochem Biophys Res Commun. 2005 May 20;330(4):1116-26. PMID:15823559[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Chen X, Li Y, Tong X, Zhang N, Wu G, Zhang Q, Wu H. Solution structure of BmP08, a novel short-chain scorpion toxin from Buthus martensi Karsch. Biochem Biophys Res Commun. 2005 May 20;330(4):1116-26. PMID:15823559 doi:S0006-291X(05)00567-X
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