View source for 1eci


==ECTATOMIN (WATER SOLUTION, NMR 20 STRUCTURES)==
<StructureSection load='1eci' size='340' side='right'caption='[[1eci]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1eci]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ectatomma_tuberculatum Ectatomma tuberculatum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ECI 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=1eci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eci OCA], [https://pdbe.org/1eci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eci RCSB], [https://www.ebi.ac.uk/pdbsum/1eci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eci ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TX1AA_ECTTU TX1AA_ECTTU] Algogenic for animals, human and insects (PubMed:7826413). At high concentrations (0.5-1 uM), it acts as a pore-forming protein that forms nonselective cation channels both in cell and artificial membranes (PubMed:7826413). It is weakly selective for cation over anions channel conductance is identical in both directions. At lower concentrations (1-10 nM), this heterodimer inhibits cardiac L-type calcium currents in isolated rat cardiac ventricular myocytes (PubMed:10336635).<ref>PMID:10336635</ref> <ref>PMID:7826413</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two-dimensional 1H NMR techniques were used to determine the spatial structure of ectatomin, a toxin from the venom of the ant Ectatomma tuberculatum. Nearly complete proton resonance assignments for two chains of ectatomin (37 and 34 amino acid residues, respectively) were obtained using 2D TOCSY, DQF-COSY and NOESY experiments. The cross-peak volumes in NOESY spectra were used to define the local structure of the protein and generate accurate proton-proton distance constraints employing the MARDIGRAS program. Disulfide bonds were located by analyzing the global fold of ectatomin, calculated with the distance geometry program DIANA. These data, combined with data on the rate of exchange of amide protons with deuterium, were used to obtain a final set of 20 structures by DIANA. These structures were refined by unrestrained energy minimization using the CHARMm program. The resulting rms deviations over 20 structures (excluding the mobile N- and c-termini of each chain) are 0.75 A for backbone heavy atoms, and 1.25 A for all heavy atoms. The conformations of the two chains are similar. Each chain consists of two alpha-helices and a hinge region of four residues; this forms a hairpin structure which is stabilized by disulfide bridges. The hinge regions of the two chains are connected together by a third disulfide bridge. Thus, ectatomin forms a four-alpha-helical bundle structure.

Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom.,Nolde DE, Sobol AG, Pluzhnikov KA, Grishin EV, Arseniev AS J Biomol NMR. 1995 Jan;5(1):1-13. PMID:7881269<ref>PMID:7881269</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1eci" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ectatomma tuberculatum]]
[[Category: Large Structures]]
[[Category: Arseniev AS]]
[[Category: Grishin EV]]
[[Category: Nolde DE]]
[[Category: Pluzhnikov KA]]
[[Category: Sobol AG]]