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1omy

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Crystal Structure of a Recombinant alpha-insect Toxin BmKaIT1 from the scorpion Buthus martensii Karsch

Structural highlights

1omy is a 1 chain structure with sequence from Mesobuthus martensii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SC12_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 (By similarity). Shows a high toxicity toward insects and moderate toxicity against mammals.^[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

Alpha-insect scorpion toxins are a distinct group of scorpion neurotoxins for which no crystal structures are yet available. A novel alpha-insect toxin named BmKalphaIT1 from the scorpion Buthus martensii Karsch (BmK) has been expressed as an inclusion body in Escherichia coli and purified by chromatography after renaturation. Recombinant BmKalphaIT1 (rBmKaIT1) was crystallized using the vapour-diffusion technique in hanging drops at 296 K. The crystals, which were grown in sodium phosphate, belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 30.24 (1), b = 36.51 (3), c = 57.08 (2) A. Diffraction data were collected to 2.1 A resolution using synchrotron radiation. There appears to be one rBmKalphaIT1 molecule in the asymmetric unit.

Crystallization and preliminary crystallographic study of rBmKalphaIT1, a recombinant alpha-insect toxin from the scorpion Buthus martensii Karsch.,Huang Y, Huang Q, Chen H, Tang Y, Miyake H, Kusunoki M Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1635-6. Epub 2003, Aug 19. PMID:12925796^[3]

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

References

↑ Huang Y, Huang Q, Chen H, Tang Y, Miyake H, Kusunoki M. Crystallization and preliminary crystallographic study of rBmKalphaIT1, a recombinant alpha-insect toxin from the scorpion Buthus martensii Karsch. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1635-6. Epub 2003, Aug 19. PMID:12925796
↑ Tong X, Zhu J, Ma Y, Chen X, Wu G, He F, Cao C, Wu H. Solution structure of BmKalphaIT01, an alpha-insect toxin from the venom of the Chinese scorpion Buthus martensii Karsch. Biochemistry. 2007 Oct 9;46(40):11322-30. Epub 2007 Sep 18. PMID:17877370 doi:10.1021/bi7006788
↑ Huang Y, Huang Q, Chen H, Tang Y, Miyake H, Kusunoki M. Crystallization and preliminary crystallographic study of rBmKalphaIT1, a recombinant alpha-insect toxin from the scorpion Buthus martensii Karsch. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1635-6. Epub 2003, Aug 19. PMID:12925796

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1omy"

@@ Line 3: / Line 3: @@
 <StructureSection load='1omy' size='340' side='right'caption='[[1omy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1omy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buthus_martensi Buthus martensi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OMY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1omy]] 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=1OMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OMY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1omy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omy OCA], [http://pdbe.org/1omy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1omy RCSB], [http://www.ebi.ac.uk/pdbsum/1omy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1omy ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=1omy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omy OCA], [https://pdbe.org/1omy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1omy RCSB], [https://www.ebi.ac.uk/pdbsum/1omy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1omy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SC12_MESMA SC12_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 (By similarity). Shows a high toxicity toward insects and moderate toxicity against mammals.<ref>PMID:12925796</ref> <ref>PMID:17877370</ref>
+[https://www.uniprot.org/uniprot/SC12_MESMA SC12_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 (By similarity). Shows a high toxicity toward insects and moderate toxicity against mammals.<ref>PMID:12925796</ref> <ref>PMID:17877370</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Buthus martensi]]
 [[Category: Large Structures]]
-[[Category: Chen, H]]
+[[Category: Mesobuthus martensii]]
-[[Category: Huang, Q]]
+[[Category: Chen H]]
-[[Category: Huang, Y]]
+[[Category: Huang Q]]
-[[Category: Kusunoki, M]]
+[[Category: Huang Y]]
-[[Category: Miyake, H]]
+[[Category: Kusunoki M]]
-[[Category: Tang, Y]]
+[[Category: Miyake H]]
-[[Category: Alpha-insect toxin]]
+[[Category: Tang Y]]
-[[Category: Sodium channel]]
-[[Category: Toxin]]

1omy

From Proteopedia

Current revision

Crystal Structure of a Recombinant alpha-insect Toxin BmKaIT1 from the scorpion Buthus martensii Karsch

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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